The many functions of ESCRTs
Abstract
Cellular membranes can form two principally different involutions, which either exclude or contain cytosol. The 'classical' budding reactions, such as those occurring during endocytosis or formation of exocytic vesicles, involve proteins that assemble on the cytosol-excluding face of the bud neck. Inverse membrane involution occurs in a wide range of cellular processes, supporting cytokinesis, endosome maturation, autophagy, membrane repair and many other processes. Such inverse membrane remodelling is mediated by a heteromultimeric protein machinery known as endosomal sorting complex required for transport (ESCRT). ESCRT proteins assemble on the cytosolic (or nucleoplasmic) face of the neck of the forming involution and cooperate with the ATPase VPS4 to drive membrane scission or sealing. Here, we review similarities and differences of various ESCRT-dependent processes, with special emphasis on mechanisms of ESCRT recruitment.
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ESCRT-III membrane scission machinery is recruited by ALIX and ESCRT-I to scission sites.
“This final event is carried out by the ESCRT-III membrane scission machinery that is recruited by ALIX and ESCRT-I to these scission sites (for review, see [16]).”
From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [16]
Cites
Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works
Shedding light on the cell biology of extracellular vesicles
van Niel, G., D'Angelo, G., & Raposo, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.125 · Cited by 8,369 · see citing works
Syndecan–syntenin–ALIX regulates the biogenesis of exosomes
Baietti, M. F., Zhang, Z., Mortier, E., Melchior, A., Degeest, G., Geeraerts, A., Ivarsson, Y., Depoortere, F., Coomans, C., Vermeiren, E., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2502 · Cited by 1,899 · see citing works
Katzmann, D. J., Babst, M., & Emr, S. D. (2001) · Cell · doi:10.1016/s0092-8674(01)00434-2 · Cited by 1,430 · see citing works
The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
Raiborg, C., & Stenmark, H. (2009) · Nature · doi:10.1038/nature07961 · Cited by 1,408 · see citing works
Self-citationTsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369 · see citing works
Itakura, E., Kishi‐Itakura, C., & Mizushima, N. (2012) · Cell · doi:10.1016/j.cell.2012.11.001 · Cited by 1,327 · see citing works
Nuclear envelope rupture and repair during cancer cell migration
Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318 · see citing works
DNA breaks and chromosome pulverization from errors in mitosis
Crasta, K., Ganem, N. J., Dagher, R., Lantermann, A. B., Ivanova, E. V., Pan, Y., Nezi, L., Protopopov, A., Chowdhury, D., & Pellman, D. (2012) · Nature · doi:10.1038/nature10802 · Cited by 1,227 · see citing works
Localization of phosphatidylinositol 3‐phosphate in yeast and mammalian cells
Gillooly, D. J., Morrow, I. C., Lindsay, M. R., Gould, R., Bryant, N. J., Gaullier, J., Parton, R. G., & Stenmark, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4577 · Cited by 1,125 · see citing works
Self-citationGibbings, D., Ciaudo, C., Erhardt, M., & Voinnet, O. (2009) · Nature Cell Biology · doi:10.1038/ncb1929 · Cited by 990 · see citing works
ESCRT III repairs nuclear envelope ruptures during cell migration to limit DNA damage and cell death
Raab, M., Gentili, M., Belly, H. D., Thiam, H. R., Vargas, P., Jiménez, A. J., Lautenschläger, F., Voituriez, R., Lennon‐Duménil, A., Manel, N., et al. (2016) · Science · doi:10.1126/science.aad7611 · Cited by 946 · see citing works
The lysosome as a cellular centre for signalling, metabolism and quality control
Lawrence, R. E., & Zoncu, R. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0244-7 · Cited by 920 · see citing works
Microautophagy of Cytosolic Proteins by Late Endosomes
Sahu, R., Kaushik, S., Clement, C. C., Cannizzo, E. S., Scharf, B., Follenzi, A., Potolicchio, I., Nieves, E., Cuervo, A. M., & Santambrogio, L. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.12.003 · Cited by 902 · see citing works
Babst, M., Katzmann, D. J., Estepa, E. J., Meerloo, T., & Emr, S. D. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00220-4 · Cited by 875 · see citing works
AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding
Strack, B., Calistri, A., Craig, S., Popova, E., & Göttlinger, H. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00653-6 · Cited by 825 · see citing works
Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia
Skibinski, G., Parkinson, N. J., Brown, J. M., Chakrabarti, L., Lloyd, S. L., Hummerich, H., Nielsen, J. E., Hodges, J. R., Spillantini, M. G., Thusgaard, T., et al. (2005) · Nature Genetics · doi:10.1038/ng1609 · Cited by 822 · see citing works
Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
Wollert, T., & Hurley, J. H. (2010) · Nature · doi:10.1038/nature08849 · Cited by 804 · see citing works
Babst, M., Wendland, B., Estepa, E. J., & Emr, S. D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.2982 · Cited by 770 · see citing works
Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery
Carlton, J. G., & Martin-Serrano, J. (2007) · Science · doi:10.1126/science.1143422 · Cited by 764 · see citing works
Catastrophic nuclear envelope collapse in cancer cell micronuclei
Hatch, E. M., Fischer, A. H., Deerinck, T. J., & Hetzer, M. W. (2013) · Cell · doi:10.1016/j.cell.2013.06.007 · Cited by 741 · see citing works
ESCRT-dependent membrane repair negatively regulates pyroptosis downstream of GSDMD activation
Rühl, S., Shkarina, K., Demarco, B., Heilig, R., Santos, J. C., & Brož, P. (2018) · Science · doi:10.1126/science.aar7607 · Cited by 740 · see citing works
Multivesicular Endosome Biogenesis in the Absence of ESCRTs
Stuffers, S., Wegner, C. S., Stenmark, H., & Brech, A. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00920.x · Cited by 731 · see citing works
Self-citationModification of intracellular membrane structures for virus replication
Miller, S., & Krijnse‐Locker, J. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1890 · Cited by 724 · see citing works
Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
Morita, E., Sandrin, V., Chung, H., Morham, S. G., Gygi, S. P., Rodesch, C. K., & Sundquist, W. I. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601850 · Cited by 724 · see citing works
Nabhan, J. F., Hu, R., Oh, R. S., Cohen, S. N., & Lu, Q. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200448109 · Cited by 722 · see citing works
Martin-Serrano, J., Zang, T., & Bieniasz, P. D. (2001) · Nature Medicine · doi:10.1038/nm1201-1313 · Cited by 710 · see citing works
ESCRT-III Acts Downstream of MLKL to Regulate Necroptotic Cell Death and Its Consequences
Gong, Y.-N., Guy, C., Olauson, H., Becker, J. U., Yang, M., Fitzgerald, P., Linkermann, A., & Green, D. R. (2017) · Cell · doi:10.1016/j.cell.2017.03.020 · Cited by 689 · see citing works
Chromothripsis and Kataegis Induced by Telomere Crisis
Maciejowski, J., Li, Y., Bosco, N., Campbell, P. J., & de Lange, T. (2015) · Cell · doi:10.1016/j.cell.2015.11.054 · Cited by 675 · see citing works
ESCRT Machinery Is Required for Plasma Membrane Repair
Jiménez, A. J., Maiuri, P., Lafaurie-Janvore, J., Divoux, S., Piel, M., & Perez, F. (2014) · Science · doi:10.1126/science.1247136 · Cited by 670 · see citing works
Hurley, J. H. (2015) · The EMBO Journal · doi:10.15252/embj.201592484 · Cited by 668 · see citing works
Babst, M., Katzmann, D. J., Snyder, W. B., Wendland, B., & Emr, S. D. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00219-8 · Cited by 662 · see citing works
Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury
Maejima, I., Takahashi, A., Omori, H., Kimura, T., Takabatake, Y., Saitoh, T., Yamamoto, A., Hamasaki, M., Noda, T., Isaka, Y., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.171 · Cited by 642 · see citing works
Filimonenko, M., Stuffers, S., Raiborg, C., Yamamoto, A., Malerød, L., Fisher, E. M. C., Isaacs, A., Brech, A., Stenmark, H., & Simonsen, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200702115 · Cited by 626 · see citing works
Self-citationRegulation of Clathrin-Mediated Endocytosis
Mettlen, M., Chen, P.-H., Srinivasan, S., Danuser, G., & Schmid, S. L. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012644 · Cited by 614 · see citing works
Aurora B-Mediated Abscission Checkpoint Protects against Tetraploidization
Steigemann, P., Wurzenberger, C., Schmitz, M. H. A., Held, M., Guizetti, J., Maar, S., & Gerlich, D. W. (2009) · Cell · doi:10.1016/j.cell.2008.12.020 · Cited by 610 · see citing works
VerPlank, L., Bouamr, F., LaGrassa, T. J., Agresta, B., Kikonyogo, A., Leis, J., & Carter, C. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.131059198 · Cited by 584 · see citing works
D'Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. W. (2009) · Cell · doi:10.1016/j.cell.2008.11.037 · Cited by 565 · see citing works
Virus budding and the ESCRT pathway
Votteler, J., & Sundquist, W. I. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.08.012 · Cited by 547 · see citing works
pH-dependent regulation of lysosomal calcium in macrophages
Christensen, K., Myers, J. T., & Swanson, J. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.3.599 · Cited by 537 · see citing works
Triggered recruitment of ESCRT machinery promotes endolysosomal repair
Skowyra, M. L., Schlesinger, P. H., Naismith, T. V., & Hanson, P. I. (2018) · Science · doi:10.1126/science.aar5078 · Cited by 537 · see citing works
Cortical Constriction During Abscission Involves Helices of ESCRT-III–Dependent Filaments
Guizetti, J., Schermelleh, L., Mäntler, J., Maar, S., Poser, I., Leonhardt, H., Müller-Reichert, T., & Gerlich, D. (2011) · Science · doi:10.1126/science.1201847 · Cited by 496 · see citing works
Orchestrating nuclear envelope disassembly and reassembly during mitosis
Güttinger, S., Laurell, E., & Kutay, U. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2641 · Cited by 480 · see citing works
Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
Bache, K. G., Brech, A., Mehlum, A., & Stenmark, H. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302131 · Cited by 470 · see citing works
Self-citationCellular Functions and Molecular Mechanisms of the ESCRT Membrane-Scission Machinery
Christ, L., Raiborg, C., Wenzel, E. M., Campsteijn, C., & Stenmark, H. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.016 · Cited by 456 · see citing works
Self-citationVps27 recruits ESCRT machinery to endosomes during MVB sorting
Katzmann, D. J., Stefan, C. J., Babst, M., & Emr, S. D. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302136 · Cited by 455 · see citing works
Herpesviruses remodel host membranes for virus egress
Johnson, D. C., & Baines, J. D. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2559 · Cited by 451 · see citing works
Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
Hanson, P. I., Roth, R., Lin, Y., & Heuser, J. E. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200707031 · Cited by 427 · see citing works
Reverse-topology membrane scission by the ESCRT proteins
Schöneberg, J., Lee, I., Iwasa, J., & Hurley, J. H. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.121 · Cited by 426 · see citing works
ESCRT-mediated lysosome repair precedes lysophagy and promotes cell survival
Radulovic, M., Bongiovanni, A., Schink, K., Nähse, V., Wenzel, E. M., Lafont, F., & Stenmark, H. (2018) · bioRxiv · doi:10.15252/embj.201899753 · Cited by 423 · see citing works
Self-citationHrs recruits clathrin to early endosomes
Raiborg, C., Bache, K. G., Mehlum, A., Stang, E., & Stenmark, H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.5008 · Cited by 389 · see citing works
Self-citationElia, N., Sougrat, R., Spurlin, T. A., Hurley, J. H., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102714108 · Cited by 389 · see citing works
Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing
Vietri, M., Schink, K. O., Campsteijn, C., Wegner, C. S., Schultz, S. W., Christ, L., Thoresen, S. B., Brech, A., Raiborg, C., & Stenmark, H. (2015) · Nature · doi:10.1038/nature14408 · Cited by 378 · see citing works
Self-citationA Role for the ESCRT System in Cell Division in Archaea
Samson, R. Y., Obita, T., Freund, S. M. V., Williams, R. L., & Bell, S. D. (2008) · Science · doi:10.1126/science.1165322 · Cited by 368 · see citing works
An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure
Takahashi, Y., He, H., Tang, Z., Hattori, T., Liu, Y., Young, M. M., Serfass, J. M., Chen, L., Gebru, M. T., Chen, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05254-w · Cited by 365 · see citing works
ESCRT-III controls nuclear envelope reformation
Olmos, Y., Hodgson, L. R., Mantell, J., Verkade, P., & Carlton, J. G. (2015) · Nature · doi:10.1038/nature14503 · Cited by 362 · see citing works
Mechanism of Ca2+-triggered ESCRT assembly and regulation of cell membrane repair
Scheffer, L., Sreetama, S. C., Sharma, N., Medikayala, S., Brown, K. J., Defour, A., & Jaiswal, J. K. (2014) · Nature Communications · doi:10.1038/ncomms6646 · Cited by 358 · see citing works
GWAS meta-analysis and replication identifies three new susceptibility loci for ovarian cancer
Study, A. C., Pharoah, P. D. P., Australian Ovarian Cancer Study Group, Tsai, Y.-Y., Ramus, S. J., Phelan, C. M., Goode, E. L., Lawrenson, K., Buckley, M. A., Fridley, B. L., et al. (2013) · Nature Genetics · doi:10.1038/ng.2564 · Cited by 341 · see citing works
Damage control: cellular mechanisms of plasma membrane repair
Andrews, N. W., de Almeida, P. E., & Corrotte, M. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.008 · Cited by 340 · see citing works
Teis, D., Saksena, S., & Emr, S. D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.08.013 · Cited by 338 · see citing works
ESCRTs and Fab1 Regulate Distinct Steps of Autophagy
Rusten, T. E., Vaccari, T., Lindmo, K., Rodahl, L. M., Nezis, I. P., Sem-Jacobsen, C., Wendler, F., Vincent, J., Brech, A., Bilder, D. H., et al. (2007) · Current Biology · doi:10.1016/j.cub.2007.09.032 · Cited by 332 · see citing works
Self-citationRelaxation of Loaded ESCRT-III Spiral Springs Drives Membrane Deformation
Chiaruttini, N., Redondo‐Morata, L., Colom, A., Humbert, F., Lenz, M., Simon Scheuring, A., & Roux, A. (2015) · Cell · doi:10.1016/j.cell.2015.10.017 · Cited by 331 · see citing works
ESCRT-III recognition by VPS4 ATPases
Stuchell‐Brereton, M. D., Skalicky, J. J., Kieffer, C., Karren, M. A., Ghaffarian, S., & Sundquist, W. I. (2007) · Nature · doi:10.1038/nature06172 · Cited by 329 · see citing works
ESCRT-III Governs the Aurora B–Mediated Abscission Checkpoint Through CHMP4C
Carlton, J. G., Caballe, A., Agromayor, M., Kloc, M., & Martin‐Serrano, J. (2012) · Science · doi:10.1126/science.1217180 · Cited by 326 · see citing works
STAM and Hrs Are Subunits of a Multivalent Ubiquitin-binding Complex on Early Endosomes
Bache, K. G., Raiborg, C., Mehlum, A., & Stenmark, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210843200 · Cited by 324 · see citing works
Self-citationALIX and the multivesicular endosome: ALIX in Wonderland
Bissig, C., & Gruenberg, J. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.10.009 · Cited by 323 · see citing works
FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes
Raiborg, C., Bremnes, B., Mehlum, A., Gillooly, D. J., D’Arrigo, A., Stang, E., & Stenmark, H. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.12.2255 · Cited by 319 · see citing works
Self-citationTSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation
Lu, Q., Hope, L. W., Brasch, M. A., Reinhard, C., & Cohen, S. N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0932599100 · Cited by 319 · see citing works
Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding
Fisher, R. D., Chung, H.-Y., Zhai, Q., Robinson, H., Sundquist, W. I., & Hill, C. P. (2007) · Cell · doi:10.1016/j.cell.2007.01.035 · Cited by 315 · see citing works
Regulation of ubiquitin-binding proteins by monoubiquitination
Hoeller, D., Crosetto, N., Blagoev, B., Raiborg, C., Tikkanen, R., Wagner, S., Kowanetz, K., Rainer Breitling, A., Mann, M., Stenmark, H., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1354 · Cited by 314 · see citing works
Self-citationNorden, C., Mendoza, M., Dobbelaere, J., Kotwaliwale, C. V., Biggins, S., & Barral, Y. (2006) · Cell · doi:10.1016/j.cell.2006.01.045 · Cited by 304 · see citing works
Amerik, A. Y., Nowak, J. A., Swaminathan, S., & Hochstrasser, M. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.10.3365 · Cited by 298 · see citing works
Functional Reconstitution of ESCRT-III Assembly and Disassembly
Saksena, S., Wahlman, J., Teis, D., Johnson, A. E., & Emr, S. D. (2009) · Cell · doi:10.1016/j.cell.2008.11.013 · Cited by 296 · see citing works
Cytokinetic Abscission: Molecular Mechanisms and Temporal Control
Mierzwa, B. E., & Gerlich, D. W. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.11.006 · Cited by 289 · see citing works
Structure and membrane remodeling activity of ESCRT-III helical polymers
McCullough, J., Clippinger, A. K., Talledge, N., Skowyra, M. L., Saunders, M. G., Naismith, T. V., Colf, L. A., Afonine, P. V., Arthur, C. P., Sundquist, W. I., et al. (2015) · Science · doi:10.1126/science.aad8305 · Cited by 283 · see citing works
Starvation induces rapid degradation of selective autophagy receptors by endosomal microautophagy
Mejlvang, J., Olsvik, H. L., Svenning, S., Bruun, J., Abudu, Y. P., Larsen, K. B., Brech, A., Hansen, T. E., Brenne, H. B., Hansen, T., et al. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201711002 · Cited by 281 · see citing works
Self-citationCytokinesis defects and cancer
Lens, S. M. A., & Medema, R. H. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0084-6 · Cited by 266 · see citing works
Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55
Lee, H. H., Elia, N., Ghirlando, R., Lippincott‐Schwartz, J., & Hurley, J. H. (2008) · Science · doi:10.1126/science.1162042 · Cited by 260 · see citing works
HIV Gag mimics the Tsg101-recruiting activity of the human Hrs protein
Pornillos, O., Higginson, D. S., Stray, K. M., Fisher, R. D., Garrus, J. E., Payne, M., He, G.-P., Wang, H. E., Morham, S. G., & Sundquist, W. I. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302138 · Cited by 258 · see citing works
Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B
Yang, D. J., Rismanchi, N., Renvoisé, B., Lippincott‐Schwartz, J., Blackstone, C. D., & Hurley, J. H. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1512 · Cited by 256 · see citing works
Mierzwa, B. E., Chiaruttini, N., Redondo‐Morata, L., von Filseck, J. M., König, J., Larios, J., Poser, I., Müller‐Reichert, T., Simon Scheuring, A., Roux, A., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3559 · Cited by 252 · see citing works
Zhao, W.-M., Seki, A., & Fang, G. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-01-0015 · Cited by 244 · see citing works
Spastin Couples Microtubule Severing to Membrane Traffic in Completion of Cytokinesis and Secretion
Connell, J. W., Lindon, C., Luzio, J. P., & Reid, E. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00847.x · Cited by 243 · see citing works
The Endosomal Sorting Complex ESCRT-II Mediates the Assembly and Architecture of ESCRT-III Helices
Henne, W. M., Buchkovich, N. J., Zhao, Y., & Emr, S. D. (2012) · Cell · doi:10.1016/j.cell.2012.08.039 · Cited by 243 · see citing works
ESCRT-III protein requirements for HIV-1 budding
Morita, E., Sandrin, V., McCullough, J., Katsuyama, A., Baci Hamilton, I., & Sundquist, W. I. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.02.004 · Cited by 242 · see citing works
Haraguchi, T., Kojidani, T., Koujin, T., Shimi, T., Osakada, H., Mori, C., Yamamoto, A., & Hiraoka, Y. (2008) · Journal of Cell Science · doi:10.1242/jcs.033597 · Cited by 235 · see citing works
Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release
Carlton, J. G., Agromayor, M., & Martin‐Serrano, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802008105 · Cited by 233 · see citing works
ALIX-CHMP4 interactions in the human ESCRT pathway
McCullough, J., Fisher, R. D., Whitby, F. G., Sundquist, W. I., & Hill, C. P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801567105 · Cited by 233 · see citing works
Detection and Clearance of Damaged Lysosomes by the Endo-Lysosomal Damage Response and Lysophagy
Papadopoulos, C., & Meyer, H. (2017) · Current Biology · doi:10.1016/j.cub.2017.11.012 · Cited by 230 · see citing works
Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4
Webster, B. M., Colombi, P., Jäger, J., & Lusk, C. P. (2014) · Cell · doi:10.1016/j.cell.2014.09.012 · Cited by 219 · see citing works
ESCRT-mediated phagophore sealing during mitophagy
Zhen, Y., Spangenberg, H., Munson, M. J., Brech, A., Schink, K. O., Tan, K.-W., Sørensen, V., Wenzel, E. M., Radulovic, M., Engedal, N., et al. (2020) · Autophagy · doi:10.1080/15548627.2019.1639301 · Cited by 209 · see citing works
Self-citationSpastin tethers lipid droplets to peroxisomes and directs fatty acid trafficking through ESCRT-III
Chang, C.-L., Weigel, A. V., Ioannou, M. S., Pasolli, H. A., Xu, C. S., Peale, D. R., Shtengel, G., Freeman, M., Hess, H. F., Blackstone, C., et al. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201902061 · Cited by 206 · see citing works
Reid, E., Connell, J. W., Edwards, T. L., Duley, S., Brown, S. E., & Sanderson, C. M. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi003 · Cited by 202 · see citing works
HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway
Martin‐Serrano, J., Eastman, S. W., Chung, W., & Bieniasz, P. D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408155 · Cited by 201 · see citing works
Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component
Baumgärtel, V., Ivanchenko, S. V., Dupont, A., Sergeev, M., Wiseman, P. W., Kräusslich, H., Bräuchle, C., Müller, B., & Lamb, D. C. (2011) · Nature Cell Biology · doi:10.1038/ncb2215 · Cited by 200 · see citing works
LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells
Gu, M., LaJoie, D., Chen, O. S., von Appen, A., Ladinsky, M. S., Redd, M. J., Nikolova, L. S., Björkman, P. J., Sundquist, W. I., Ullman, K. S., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613916114 · Cited by 200 · see citing works
Distribution of ESCRT Machinery at HIV Assembly Sites Reveals Virus Scaffolding of ESCRT Subunits
van Engelenburg, S. B., Shtengel, G. E., Sengupta, P., Waki, K., Jarník, M., Ablan, S. D., Freed, E. O., Hess, H. F., & Lippincott‐Schwartz, J. (2014) · Science · doi:10.1126/science.1247786 · Cited by 191 · see citing works
Lafaurie-Janvore, J., Maiuri, P., Wang, I., Pinot, M., Manneville, J., Betz, T., Balland, M., & Piel, M. (2013) · Science · doi:10.1126/science.1233866 · Cited by 189 · see citing works
A Unique Role for the Host ESCRT Proteins in Replication of Tomato bushy stunt virus
Barajas, D., Jiang, Y., & Nagy, P. D. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000705 · Cited by 189 · see citing works
The ESCRT machinery regulates the secretion and long-range activity of Hedgehog
Matusek, T., Wendler, F., Polès, S., Pizette, S., D’Angelo, G., Fürthauer, M., & Thérond, P. P. (2014) · Nature · doi:10.1038/nature13847 · Cited by 184 · see citing works
Structure of the ESCRT-II endosomal trafficking complex
Hierro, A., Sun, J., Rusnak, A. S., Kim, J., Prag, G., Emr, S. D., & Hurley, J. H. (2004) · Nature · doi:10.1038/nature02914 · Cited by 182 · see citing works
Adell, M. A. Y., Vogel, G. F., Pakdel, M., Müller, M., Lindner, H. H., Hess, M. W., & Teis, D. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201310114 · Cited by 182 · see citing works
Rab5-dependent autophagosome closure by ESCRT
Zhou, F., Wu, Z., Zhao, M., Murtazina, R., Cai, J., Zhang, A., Li, R. Q., Sun, D., Li, W., Zhao, L. Q., et al. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201811173 · Cited by 179 · see citing works
Governance of Endocytic Trafficking and Signaling by Reversible Ubiquitylation
Clague, M. J., Liu, H., & Urbé, S. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.08.011 · Cited by 177 · see citing works
Repair of nuclear ruptures requires barrier-to-autointegration factor
Halfmann, C. T., Sears, R. M., Katiyar, A., Busselman, B. W., Aman, L., Zhang, Q., O’Bryan, C. S., Angelini, T. E., Lele, T. P., & Roux, K. J. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201901116 · Cited by 176 · see citing works
The way out: what we know and do not know about herpesvirus nuclear egress
Mettenleiter, T. C., Müller, F., Granzow, H., & Klupp, B. G. (2012) · Cellular Microbiology · doi:10.1111/cmi.12044 · Cited by 168 · see citing works
Kieffer, C., Skalicky, J. J., Morita, E., Domenico, I. D., Ward, D. M., Kaplan, J., & Sundquist, W. I. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.05.014 · Cited by 167 · see citing works
Human ESCRT-II Complex and Its Role in Human Immunodeficiency Virus Type 1 Release
Langelier, C., von Schwedler, U. K., Fisher, R. D., De Domenico, I., White, P. L., Hill, C. P., Kaplan, J., Ward, D., & Sundquist, W. I. (2006) · Journal of Virology · doi:10.1128/jvi.01049-06 · Cited by 166 · see citing works
An ESCRT–spastin interaction promotes fission of recycling tubules from the endosome
Allison, R. J., Lumb, J. H., Fassier, C., Connell, J. W., Martín, D. T., Seaman, M. N. J., Hazan, J., & Reid, E. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201211045 · Cited by 164 · see citing works
Oxidation of F-actin controls the terminal steps of cytokinesis
Frémont, S., Hammich, H., Bai, J., Wioland, H., Klinkert, K., Rocancourt, M., Kikuti, C. M., Stroebel, D., Romet‐Lemonne, G., Pylypenko, O., et al. (2017) · Nature Communications · doi:10.1038/ncomms14528 · Cited by 164 · see citing works
ALIX and ESCRT-I/II function as parallel ESCRT-III recruiters in cytokinetic abscission
Christ, L., Wenzel, E. M., Liestøl, K., Raiborg, C., Campsteijn, C., & Stenmark, H. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201507009 · Cited by 163 · see citing works
Self-citationChung, H.-Y., Morita, E., von Schwedler, U. K., Müller, B., Kräusslich, H., & Sundquist, W. I. (2008) · Journal of Virology · doi:10.1128/jvi.02667-07 · Cited by 161 · see citing works
Functional Repurposing Revealed by Comparing S. pombe and S. cerevisiae Genetic Interactions
Frost, A. S., Elgort, M., Brandman, O., Ives, C., Collins, S. R., Miller-Vedam, L. E., Weibezahn, J., Hein, M. Y., Poser, I., Mann, M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.028 · Cited by 161 · see citing works
ATP-dependent force generation and membrane scission by ESCRT-III and Vps4
Schöneberg, J., Pavlin, M., Yan, S., Righini, M., Lee, I.-H., Carlson, L., Bahrami, A., Goldman, D. H., Ren, X.-F., Hummer, G., et al. (2018) · Science · doi:10.1126/science.aat1839 · Cited by 161 · see citing works
Plk1 negatively regulates Cep55 recruitment to the midbody to ensure orderly abscission
Bastos, R. N., & Barr, F. A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201008108 · Cited by 160 · see citing works
Structural basis for viral late-domain binding to Alix
Lee, S., Joshi, A., Nagashima, K., Freed, E. O., & Hurley, J. H. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1203 · Cited by 158 · see citing works
Raiborg, C., Wesche, J., Malerød, L., & Stenmark, H. (2006) · Journal of Cell Science · doi:10.1242/jcs.02978 · Cited by 155 · see citing works
Self-citationAdell, M. A. Y., Migliano, S. M., Upadhyayula, S., Bykov, Y. S., Sprenger, S., Pakdel, M., Vogel, G. F., Jih, G. T., Skillern, W., Behrouzi, R., et al. (2017) · eLife · doi:10.7554/elife.31652 · Cited by 154 · see citing works
Structural insight into the ESCRT‐I/‐II link and its role in MVB trafficking
Gill, D. J., Teo, H., Sun, J., Perišić, O., Veprintsev, D. B., Emr, S. D., & Williams, R. L. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601501 · Cited by 150 · see citing works
Structural and functional studies of ALIX interactions with YPXnL late domains of HIV-1 and EIAV
Zhai, Q., Fisher, R. D., Chung, H.-Y., Myszka, D. G., Sundquist, W. I., & Hill, C. P. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1319 · Cited by 148 · see citing works
p53 Accumulation, defective cell proliferation, and early embryonic lethality in mice lacking tsg101
Ruland, J., Sirard, C., Elia, A., MacPherson, D. P., Wakeham, A. C., Li, L., de la Pompa, J. L., Cohen, S. N., & Mak, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1859 · Cited by 145 · see citing works
A mechanism for chromosome segregation sensing by the NoCut checkpoint
Mendoza, M., Norden, C., Durrer, K., Rauter, H., Uhlmann, F., & Barral, Y. (2009) · Nature Cell Biology · doi:10.1038/ncb1855 · Cited by 145 · see citing works
ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4
Thoresen, S. B., Campsteijn, C., Vietri, M., Schink, K. O., Liestøl, K., Andersen, J., Raiborg, C., & Stenmark, H. (2014) · Nature Cell Biology · doi:10.1038/ncb2959 · Cited by 145 · see citing works
Self-citationMembrane deformation and scission by the HSV-1 nuclear egress complex
Bigalke, J. M., Heuser, T., Nicastro, D., & Heldwein, E. E. Z. (2014) · Nature Communications · doi:10.1038/ncomms5131 · Cited by 144 · see citing works
Torsin Mediates Primary Envelopment of Large Ribonucleoprotein Granules at the Nuclear Envelope
Jokhi, V., Ashley, J., Nunnari, J. N., Noma, A., Ito, N., Wakabayashi-Ito, N., Moore, M. J., & Budnik, V. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.015 · Cited by 138 · see citing works
Essential Role of hIST1 in Cytokinesis
Agromayor, M., Carlton, J. G., Phelan, J. P., Matthews, D. R., Carlin, L. M., Ameer‐Beg, S., Bowers, K., & Martin‐Serrano, J. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0474 · Cited by 138 · see citing works
Biochemical Analyses of Human IST1 and Its Function in Cytokinesis
Bajorek, M., Morita, E., Skalicky, J. J., Morham, S. G., Babst, M., & Sundquist, W. I. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0475 · Cited by 138 · see citing works
Ist1 Regulates Vps4 Localization and Assembly
Dimaano, C., Jones, C. B., Hanono, A., Curtiss, M., & Babst, M. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-08-0747 · Cited by 137 · see citing works
Arabidopsis TOL Proteins Act as Gatekeepers for Vacuolar Sorting of PIN2 Plasma Membrane Protein
Korbei, B., Moulinier‐Anzola, J., De-Araújo, L., Lucyshyn, D., Retzer, K., Khan, M. A., & Luschnig, C. (2013) · Current Biology · doi:10.1016/j.cub.2013.10.036 · Cited by 137 · see citing works
Unrestrained ESCRT-III drives micronuclear catastrophe and chromosome fragmentation
Vietri, M., Schultz, S. W., Bellanger, A., Jones, C. M., Petersen, L. I., Raiborg, C., Skarpen, E., Pedurupillay, C. R. J., Kjos, I., Kip, E., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0537-5 · Cited by 133 · see citing works
Self-citationMembrane Binding by CHMP7 Coordinates ESCRT-III-Dependent Nuclear Envelope Reformation
Olmos, Y., Perdrix-Rosell, A., & Carlton, J. G. (2016) · Current Biology · doi:10.1016/j.cub.2016.07.039 · Cited by 132 · see citing works
López-Jiménez, A. T., Cardenal‐Muñoz, E., Leuba, F., Gerstenmaier, L., Barisch, C., Hagedorn, M., King, J., & Soldati, T. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007501 · Cited by 132 · see citing works
Capalbo, L., Montembault, É., Takeda, T., Bassi, Z. I., Glover, D. M., & D’Avino, P. P. (2012) · Open Biology · doi:10.1098/rsob.120070 · Cited by 130 · see citing works
Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing
Webster, B. M., Thaller, D. J., Jäger, J., Ochmann, S. E., Borah, S., & Lusk, C. P. (2016) · The EMBO Journal · doi:10.15252/embj.201694574 · Cited by 129 · see citing works
CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling
Yan, Q., Sun, W., Kujala, P., Lotfi, Y., Vida, T. A., & Bean, A. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-11-1014 · Cited by 128 · see citing works
ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins
Caballe, A., Wenzel, D. M., Agromayor, M., Alam, S. L., Skalicky, J. J., Kloc, M., Carlton, J. G., Labrador, L., Sundquist, W. I., & Martin‐Serrano, J. (2015) · eLife · doi:10.7554/elife.06547 · Cited by 125 · see citing works
UBAP1 Is a Component of an Endosome-Specific ESCRT-I Complex that Is Essential for MVB Sorting
Stefani, F., Zhang, L., Taylor, S., Donovan, J., Rollinson, S. J., Doyotte, A., Brownhill, K., Callister, J. B., Pickering-Brown, S. M., & Woodman, P. G. (2011) · Current Biology · doi:10.1016/j.cub.2011.06.028 · Cited by 122 · see citing works
Molecular and Structural Basis of ESCRT-III Recruitment to Membranes during Archaeal Cell Division
Samson, R. Y., Obita, T., Hodgson, B., Shaw, M. K., Chong, P. L., Williams, R. L., & Bell, S. D. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.018 · Cited by 121 · see citing works
Wenzel, E. M., Schultz, S. W., Schink, K. O., Pedersen, N. M., Nähse, V., Carlson, A., Brech, A., Stenmark, H., & Raiborg, C. (2018) · Nature Communications · doi:10.1038/s41467-018-05345-8 · Cited by 121 · see citing works
Self-citationBarajas, D., de Castro, I. F., Pogany, J., Risco, C., & Nagy, P. D. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004087 · Cited by 120 · see citing works
Lee, C., Liu, P.-T., Kung, H., Su, M.-T., Chua, H., Chang, Y.-H., Chang, C.-W., Tsai, C.-H. A., Liu, F., & Chen, M. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002904 · Cited by 118 · see citing works
Endosomal membrane tension regulates ESCRT-III-dependent intra-lumenal vesicle formation
Mercier, V., Larios, J., Molinard, G., Goujon, A., Matile, S., Gruenberg, J. E., & Roux, A. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0546-4 · Cited by 118 · see citing works
Breaching the nuclear envelope in development and disease
Hatch, E. M., & Hetzer, M. W. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201402003 · Cited by 116 · see citing works
Structural and Functional Organization of the ESCRT-I Trafficking Complex
Kostelansky, M. S., Sun, J., Lee, S., Kim, J., Ghirlando, R., Hierro, A., Emr, S. D., & Hurley, J. H. (2006) · Cell · doi:10.1016/j.cell.2006.01.049 · Cited by 115 · see citing works
Endocytic membrane fusion and buckling-induced microtubule severing mediate cell abscission
Schiel, J. A., Park, K., Morphew, M. K., Reid, E., Hoenger, A., & Prekeris, R. (2011) · Journal of Cell Science · doi:10.1242/jcs.081448 · Cited by 114 · see citing works
ESCRT-III mediates budding across the inner nuclear membrane and regulates its integrity
Arii, J., Watanabe, M., Maeda, F., Tokai-Nishizumi, N., Chihara, T., Miura, M., Maruzuru, Y., Koyanagi, N., Kato, A., & Kawaguchi, Y. (2018) · Nature Communications · doi:10.1038/s41467-018-05889-9 · Cited by 113 · see citing works
Temporal and spatial organization of ESCRT protein recruitment during HIV-1 budding
Bleck, M., Itano, M. S., Johnson, D. S., Thomas, V. K., North, A. J., Bieniasz, P. D., & Simon, S. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321655111 · Cited by 112 · see citing works
Unique Requirement for ESCRT Factors in Flavivirus Particle Formation on the Endoplasmic Reticulum
Tabata, K., Arimoto, M., Arakawa, M., Nara, A., Saito, K., Omori, H., Arai, A., Ishikawa, T., Konishi, E., Suzuki, R., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.068 · Cited by 112 · see citing works
Usami, Y., Popov, S. V., Popova, E. N., & Göttlinger, H. G. (2008) · Journal of Virology · doi:10.1128/jvi.02675-07 · Cited by 110 · see citing works
Mittal, E., Skowyra, M. L., Uwase, G., Tinaztepe, E., Mehra, A., Köster, S., Hanson, P. I., & Philips, J. A. (2018) · mBio · doi:10.1128/mbio.01765-18 · Cited by 110 · see citing works
Thaller, D. J., Allegretti, M., Borah, S., Ronchi, P., Beck, M., & Lusk, C. P. (2019) · eLife · doi:10.7554/elife.45284 · Cited by 109 · see citing works
An ESCRT module is required for neuron pruning
Loncle, N., Agromayor, M., Martin‐Serrano, J., & Williams, D. W. (2015) · Scientific Reports · doi:10.1038/srep08461 · Cited by 108 · see citing works
Defects in nuclear pore assembly lead to activation of an Aurora B–mediated abscission checkpoint
Mackay, D. R., Makise, M., & Ullman, K. S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201007124 · Cited by 108 · see citing works
Annexin A7 is required for ESCRT III-mediated plasma membrane repair
Sønder, S. L., Boye, T. L., Tölle, R. C., Dengjel, J., Maeda, K., Jäättelä, M., Simonsen, A. C., Jaiswal, J. K., & Nylandsted, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-43143-4 · Cited by 108 · see citing works
The UBAP1 Subunit of ESCRT-I Interacts with Ubiquitin via a SOUBA Domain
Agromayor, M., Soler, N., Caballe, A., Kueck, T., Freund, S. M. V., Allen, M. D., Bycroft, M., Perišić, O., Ye, Y., McDonald, B., et al. (2012) · Structure · doi:10.1016/j.str.2011.12.013 · Cited by 105 · see citing works
Visualization of long-lived proteins reveals age mosaicism within nuclei of postmitotic cells
Toyama, B. H., Drigo, R. A. E., Lev‐Ram, V., Ramachandra, R., Deerinck, T. J., Lechène, C., Ellisman, M. H., & Hetzer, M. W. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201809123 · Cited by 103 · see citing works
Host ESCRT Proteins Are Required for Bromovirus RNA Replication Compartment Assembly and Function
Diaz, A., Zhang, J., Abigail, O., Wang, X., & Ahlquist, P. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004742 · Cited by 101 · see citing works
Mayers, J. R., Fyfe, I., Schuh, A. L., Chapman, E. R., Edwardson, J. M., & Audhya, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185363 · Cited by 100 · see citing works
Han, Z., Lu, J., Liu, Y., Davis, B., Lee, M. S., Olson, M. A., Ruthel, G. T., Freedman, B. D., Schnell, M. J., Wrobel, J. E., et al. (2014) · Journal of Virology · doi:10.1128/jvi.00591-14 · Cited by 100 · see citing works
Pashkova, N., Gakhar, L., Winistorfer, S. C., Sunshine, A. B., Rich, M. S., Dunham, M. J., Yu, L. P., & Piper, R. C. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.04.007 · Cited by 94 · see citing works
Zhang, H., Wang, Y., Wong, J. J. L., Lim, K., Liou, Y., Wang, H., & Yu, F. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.014 · Cited by 94 · see citing works
Resolving ESCRT-III Spirals at the Intercellular Bridge of Dividing Cells Using 3D STORM
Goliand, I., Adar-Levor, S., Segal, I., Nachmias, D., Dadosh, T., Kozlov, M. M., & Elia, N. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.051 · Cited by 87 · see citing works
Zeev‐Ben‐Mordehai, T., Weberruss, M. H., Lorenz, M., Cheleski, J., Hellberg, T., Whittle, C., Omari, K. E., Vasishtan, D., Dent, K. C., Harlos, K., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.008 · Cited by 86 · see citing works
Growing functions of the ESCRT machinery in cell biology and viral replication.
Scourfield, E., & Martin-Serrano, J. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160479 · Cited by 85 · see citing works
CC2D1B Coordinates ESCRT-III Activity during the Mitotic Reformation of the Nuclear Envelope
Ventimiglia, L. N., Cuesta-Geijo, M. Á., Martinelli, N., Caballe, A., Machebœuf, P., Miguet, N., Parnham, I. M., Olmos, Y., Carlton, J. G., Weissenhorn, W., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.11.012 · Cited by 85 · see citing works
ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro1 during MVB biogenesis
Tang, S., Buchkovich, N. J., Henne, W. M., Banjade, S., Kim, Y. J., & Emr, S. D. (2016) · eLife · doi:10.7554/elife.15507 · Cited by 84 · see citing works
Willan, J., Cleasby, A. J., Rodriguez, N. F., Stefani, F., Rinaldo, C., Pisciottani, A., Grant, E. K., Woodman, P. G., Bryant, H. E., & Ciani, B. (2019) · Oncogenesis · doi:10.1038/s41389-019-0136-0 · Cited by 83 · see citing works
Timing of ESCRT-III protein recruitment and membrane scission during HIV-1 assembly
Johnson, D. S., Bleck, M., & Simon, S. M. (2018) · eLife · doi:10.7554/elife.36221 · Cited by 81 · see citing works
The α-arrestin ARRDC3 mediates ALIX ubiquitination and G protein–coupled receptor lysosomal sorting
Dores, M. R., Lin, H., Grimsey, N. J., Mendez, F., & Trejo, J. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-05-0284 · Cited by 79 · see citing works
A founder mutation in Vps37A causes autosomal recessive complex hereditary spastic paraparesis
Zivony-Elboum, Y., Westbroek, W., Kfir, N. C., Savitzki, D., Shoval, Y., Bloom, A., Rod, R., Khayat, M., Gross, B., Samri, W., et al. (2012) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2012-100742 · Cited by 79 · see citing works
Horii, M., Shibata, H., Kobayashi, R., Katoh, K., Yorikawa, C., Yasuda, J., & Maki, M. (2006) · Biochemical Journal · doi:10.1042/bj20060897 · Cited by 78 · see citing works
Sadler, J. B. A., Wenzel, D. M., Strohacker, L. K., Guindo-Martínez, M., Alam, S. L., Mercader, J. M., Torrents, D., Ullman, K. S., Sundquist, W. I., & Martin‐Serrano, J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805504115 · Cited by 77 · see citing works
ESCRT-III/Vps4 Controls Heterochromatin-Nuclear Envelope Attachments
Pieper, G. H., Sprenger, S., Teis, D., & Oliferenko, S. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.01.028 · Cited by 75 · see citing works
Katoh, K., Suzuki, H., Terasawa, Y., Mizuno, T., Yasuda, J., Shibata, H., & Maki, M. (2005) · Biochemical Journal · doi:10.1042/bj20050398 · Cited by 73 · see citing works
Weiss, E. R., Popova, E. N., Yamanaka, H., Kim, H. C., Huibregtse, J. M., & Göttlinger, H. G. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001107 · Cited by 73 · see citing works
ESCRT-III is required for scissioning new peroxisomes from the endoplasmic reticulum
Mast, F. D., Herricks, T., Strehler, K. M., Miller, L. R., Saleem, R. A., Rachubinski, R. A., & Aitchison, J. D. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201706044 · Cited by 72 · see citing works
Karasmanis, E. P., Hwang, D. H., Νάκος, Κ., Bowen, J. R., Angelis, D., & Spiliotis, E. T. (2018) · Current Biology · doi:10.1016/j.cub.2019.05.050 · Cited by 72 · see citing works
Abscission Is Regulated by the ESCRT-III Protein Shrub in Drosophila Germline Stem Cells
Matias, N. R., Mathieu, J., & Huynh, J. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1004653 · Cited by 71 · see citing works
Mackay, D. R., & Ullman, K. S. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-11-1563 · Cited by 67 · see citing works
CC2D1A Is a Regulator of ESCRT-III CHMP4B
Martinelli, N., Hartlieb, B., Usami, Y., Sabin, C., Dordor, A., Miguet, N., Avilov, S., Ribeiro, E. A., Göttlinger, H. G., & Weissenhorn, W. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.02.044 · Cited by 66 · see citing works
Association of CHMP4B and autophagy with micronuclei: implications for cataract formation
Sagona, A. P., Nezis, I. P., & Stenmark, H. (2014) · BioMed Research International · doi:10.1155/2014/974393 · Cited by 64 · see citing works
Self-citationKovalev, N., de Castro, I. F., Pogany, J., Barajas, D., Pathak, K. B., Risco, C., & Nagy, P. D. (2016) · Journal of Virology · doi:10.1128/jvi.02775-15 · Cited by 64 · see citing works
Eikenes, Å. H., Malerød, L., Lie-Jensen, A., Steen, C. B., Mathieu, J., Nezis, I. P., Liestøl, K., Huynh, J., Stenmark, H., & Haglund, K. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1004904 · Cited by 63 · see citing works
Self-citationMansilla Pareja, M. E., Bongiovanni, A., Lafont, F., & Colombo, M. I. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00112 · Cited by 62 · see citing works
The Multifunctional Ebola Virus VP40 Matrix Protein is a Promising Therapeutic Target
Madara, J. J., Han, Z., Ruthel, G. T., Freedman, B. D., & Harty, R. N. (2015) · Future Virology · doi:10.2217/fvl.15.6 · Cited by 60 · see citing works
HRS–WASH axis governs actin-mediated endosomal recycling and cell invasion
MacDonald, E., Brown, L., Selvais, A., Liu, H., Waring, T., Newman, D., Bithell, J., Grimes, D., Urbé, S., Clague, M. J., et al. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201710051 · Cited by 59 · see citing works
Dores, M. R., Grimsey, N. J., Mendez, F., & Trejo, J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157587 · Cited by 58 · see citing works
The RIF1-PP1 Axis Controls Abscission Timing in Human Cells
Bhowmick, R., Thakur, R. S., Venegas, A. B., Liu, Y., Nilsson, J., Barišić, M., & Hickson, I. D. (2019) · Current Biology · doi:10.1016/j.cub.2019.02.037 · Cited by 58 · see citing works
Inhibition of ESCRT-II–CHMP6 interactions impedes cytokinetic abscission and leads to cell death
Goliand, I., Nachmias, D., Gershony, O., & Elia, N. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-08-1317 · Cited by 57 · see citing works
Induction of autophagy in ESCRT mutants is an adaptive response for cell survival in C. elegans
Djeddi, A., Michelet, X., Culetto, E., Alberti, A., Barois, N., & Legouis, R. (2012) · Journal of Cell Science · doi:10.1242/jcs.091702 · Cited by 56 · see citing works
AP-3 regulates PAR1 ubiquitin-independent MVB/lysosomal sorting via an ALIX-mediated pathway
Dores, M. R., Paing, M. M., Lin, H., Montagne, W. A., Marchese, A., & Trejo, J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-03-0251 · Cited by 56 · see citing works
Dynein pulling forces counteract lamin-mediated nuclear stability during nuclear envelope repair
Penfield, L., Wysolmerski, B., Mauro, M. S., Farhadifar, R., Martinez, M. A. Q., Biggs, R. J., Wu, H., Broberg, C., Needleman, D. J., & Bahmanyar, S. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0374 · Cited by 55 · see citing works
Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7
Bauer, I., Brune, T., Preiss, R., & Kölling, R. (2015) · Genetics · doi:10.1534/genetics.115.178939 · Cited by 52 · see citing works
Loss of Nuclear Envelope Integrity in Aging and Disease
Robijns, J., Houthaeve, G., Braeckmans, K., & Vos, W. H. D. (2017) · International review of cytology · doi:10.1016/bs.ircmb.2017.07.013 · Cited by 52 · see citing works
Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101
Okumura, M., Ichioka, F., Kobayashi, R., SUZUKI, H., Yoshida, H., Shibata, H., & Maki, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.015 · Cited by 52 · see citing works
Functional interplay between a virus and the ESCRT machinery in Archaea
Snyder, J. C., Samson, R. Y., Brumfield, S. K., Bell, S. D., & Young, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301605110 · Cited by 51 · see citing works
Capping protein regulates actin dynamics during cytokinetic midbody maturation
Terry, S. J., Donà, F., Osenberg, P., Carlton, J. G., & Eggert, U. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722281115 · Cited by 49 · see citing works
Richardson, L. G. L., Clendening, E. A., Sheen, H., Gidda, S. K., White, K. A., & Mullen, R. T. (2014) · Journal of Virology · doi:10.1128/jvi.03840-13 · Cited by 48 · see citing works
Capalbo, L., Mela, I., Abad, M. A., Jeyaprakash, A. A., Edwardson, J. M., & D’Avino, P. P. (2016) · Open Biology · doi:10.1098/rsob.160248 · Cited by 44 · see citing works
Lee, C., Liu, G., Kung, H., Liu, P.-T., Liao, Y., Chow, L., Chang, L.-S., Chang, Y.-H., Chang, C.-W., Shu, W., et al. (2016) · Journal of Virology · doi:10.1128/jvi.01235-16 · Cited by 43 · see citing works
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Exosomes as a new frontier of cancer liquid biopsy
Yu, D. B., Li, Y., Wang, M., Gu, J., Xu, W., Cai, H., Fang, X., & Zhang, X. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01509-9 · Cited by 901 · see citing works
Mechanisms governing autophagosome biogenesis
Nakatogawa, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0241-0 · Cited by 876 · see citing works
Exosomes as mediators of intercellular crosstalk in metabolism
Isaac, R., Reis, F. C. G., Ying, W., & Olefsky, J. M. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.08.006 · Cited by 835 · see citing works
Exosome biogenesis: machinery, regulation, and therapeutic implications in cancer
Han, Q.-F., Li, W.-J., Hu, K., Gao, J., Zhai, W., Yang, J.-H., & Zhang, S. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01671-0 · Cited by 683 · see citing works
Machinery, regulation and pathophysiological implications of autophagosome maturation
Zhao, Y. G., Codogno, P., & Zhang, H. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00392-4 · Cited by 574 · see citing works
Computed structures of core eukaryotic protein complexes
Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542 · see citing works
RAB31 marks and controls an ESCRT-independent exosome pathway
Wei, D., Zhan, W., Gao, Y., Huang, L., Gong, R., Wang, W., Zhang, R., Wu, Y., Gao, S., & Kang, T. (2020) · Cell Research · doi:10.1038/s41422-020-00409-1 · Cited by 498 · see citing works
Phosphoinositides as membrane organizers
Posor, Y., Jang, W., & Haucke, V. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00490-x · Cited by 469 · see citing works
Current Strategies for Exosome Cargo Loading and Targeting Delivery
Zeng, H., Guo, S., Ren, X., Wu, Z., Liu, S., & Yao, X. (2023) · Cells · doi:10.3390/cells12101416 · Cited by 452 · see citing works
The ins-and-outs of exosome biogenesis, secretion, and internalization
Arya, S. B., Collie, S. P., & Parent, C. A. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.06.006 · Cited by 423 · see citing works
Plant-derived exosome-like nanoparticles and their therapeutic activities
Kim, J., Li, S., Zhang, S., & Wang, J. (2021) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2021.05.006 · Cited by 412 · see citing works
Shedding Light on Extracellular Vesicle Biogenesis and Bioengineering
Teng, F., & Fussenegger, M. (2020) · Advanced Science · doi:10.1002/advs.202003505 · Cited by 384 · see citing works
Recent Advances in DNA Origami-Engineered Nanomaterials and Applications
Zhan, P., Peil, A., Jiang, Q., Wang, D., Mousavi, S., Xiong, Q., Shen, Q., Shang, Y., Ding, B., Lin, C., et al. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00028 · Cited by 362 · see citing works
Autophagosome biogenesis: From membrane growth to closure
Melia, T. J., Lystad, A. H., & Simonsen, A. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202002085 · Cited by 324 · see citing works
Pyroptosis, metabolism, and tumor immune microenvironment
Du, T., Gao, J., Li, P., Wang, Y., Qi, Q., Liu, X., Li, J., Wang, C., & Du, L. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.492 · Cited by 325 · see citing works
Microautophagy – distinct molecular mechanisms handle cargoes of many sizes
Schuck, S. (2020) · Journal of Cell Science · doi:10.1242/jcs.246322 · Cited by 321 · see citing works
Lin, Z., Wu, Y., Xu, Y., Li, G., Li, Z., & Liu, T. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01650-5 · Cited by 297 · see citing works
Lysosomes as coordinators of cellular catabolism, metabolic signalling and organ physiology
Settembre, C., & Perera, R. M. (2023) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-023-00676-x · Cited by 269 · see citing works
Towards targeting of shared mechanisms of cancer metastasis and therapy resistance
Weiß, F., Lauffenburger, D. A., & Friedl, P. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-021-00427-0 · Cited by 294 · see citing works
Exploiting the biogenesis of extracellular vesicles for bioengineering and therapeutic cargo loading
Rädler, J., Gupta, D., Zickler, A. M., & Andaloussi, S. E. (2023) · Molecular Therapy · doi:10.1016/j.ymthe.2023.02.013 · Cited by 292 · see citing works
Inflammasome‐associated cell death: Pyroptosis, apoptosis, and physiological implications
Tsuchiya, K. (2020) · Microbiology and Immunology · doi:10.1111/1348-0421.12771 · Cited by 238 · see citing works
Targeting lysosomes in human disease: from basic research to clinical applications
Cao, M., Luo, X., Wu, K., & He, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00778-y · Cited by 225 · see citing works
An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission
Pfitzner, A.-K., Mercier, V., Jiang, X., von Filseck, J. M., Baum, B., Šarić, A., & Roux, A. (2020) · Cell · doi:10.1016/j.cell.2020.07.021 · Cited by 207 · see citing works
Extracellular vesicle analysis
Hendrix, A., Lippens, L., Pinheiro, C., Théry, C., Jaular, L. M., Lötvall, J. O., Lässer, C., Hill, A. F., & Witwer, K. W. (2023) · Nature Reviews Methods Primers · doi:10.1038/s43586-023-00240-z · Cited by 192 · see citing works
Autophagy and endocytosis – interconnections and interdependencies
Birgisdottir, Å. B., & Johansen, T. (2020) · Journal of Cell Science · doi:10.1242/jcs.228114 · Cited by 170 · see citing works
Autophagosome biogenesis comes out of the black box
Chang, C., Jensen, L. E., & Hurley, J. H. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00669-y · Cited by 171 · see citing works
Immune Cell-Derived Exosomes in the Cancer-Immunity Cycle
Yan, W., & Jiang, S. (2020) · Trends in cancer · doi:10.1016/j.trecan.2020.02.013 · Cited by 170 · see citing works
Wang, J., Fang, N., Xiong, J., Du, Y., Cao, Y., & Ji, W.-K. (2021) · Nature Communications · doi:10.1038/s41467-021-21525-5 · Cited by 153 · see citing works
A shared, stochastic pathway mediates exosome protein budding along plasma and endosome membranes
Fordjour, F. K., Guo, C., Ai, Y., Daaboul, G. G., & Gould, S. J. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102394 · Cited by 150 · see citing works
ESCRT-dependent STING degradation inhibits steady-state and cGAMP-induced signalling
Gentili, M., Liu, B., Papanastasiou, M., Dele-Oni, D. O., Schwartz, M. A., Carlson, R. J., Al’Khafaji, A. M., Krug, K., Brown, A., Doench, J. G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36132-9 · Cited by 149 · see citing works
Extracellular Vesicles as an Efficient and Versatile System for Drug Delivery
Dang, X. T. T., Jayasinghe, M. K., Zhang, D. X., Pirisinu, M., & Le, M. T. N. (2020) · Cells · doi:10.3390/cells9102191 · Cited by 144 · see citing works
Coyne, A. N., Baskerville, V., Zaepfel, B. L., Dickson, D. W., Rigo, F., Bennett, F., Lusk, C. P., & Rothstein, J. D. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe1923 · Cited by 143 · see citing works
Extracellular vesicles and particles impact the systemic landscape of cancer
Lucotti, S., Kenific, C. M., Zhang, H., & Lyden, D. C. (2022) · The EMBO Journal · doi:10.15252/embj.2021109288 · Cited by 134 · see citing works
Unrestrained ESCRT-III drives micronuclear catastrophe and chromosome fragmentation
Vietri, M., Schultz, S. W., Bellanger, A., Jones, C. M., Petersen, L. I., Raiborg, C., Skarpen, E., Pedurupillay, C. R. J., Kjos, I., Kip, E., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0537-5 · Cited by 133 · see citing works
Self-citationLysosomes drive the piecemeal removal of mitochondrial inner membrane
Prashar, A., Bussi, C., Fearns, A., Capurro, M., Gao, X., Sesaki, H., Gutierrez, M. G., & Jones, N. L. (2024) · Nature · doi:10.1038/s41586-024-07835-w · Cited by 139 · see citing works
Chen, Q.-T., Zhang, Z., Huang, Q., Chen, H., Hong, W., Lin, T., Zhao, W., Wang, X., Ju, C.-Y., Wu, L.-Z., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00642-5 · Cited by 141 · see citing works
Ca2+-activated sphingomyelin scrambling and turnover mediate ESCRT-independent lysosomal repair
Niekamp, P., Scharte, F., Sokoya, T., Vittadello, L., Kim, Y., Deng, Y., Südhoff, E., Hilderink, A., Imlau, M., Clarke, C. J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29481-4 · Cited by 132 · see citing works
Miceli, R. T., Chen, T.-Y., Nose, Y., Tichkule, S., Brown, B., Fullard, J. F., Saulsbury, M. D., Heyliger, S. O., Gnjatic, S., Kyprianou, N., et al. (2024) · Journal of Extracellular Vesicles · doi:10.1002/jev2.70005 · Cited by 129 · see citing works
Wu, Y., Li, J., Zeng, Y., Pu, W., Mu, X., Sun, K., Peng, Y., & Shen, B. (2022) · International Journal of Oral Science · doi:10.1038/s41368-022-00187-z · Cited by 124 · see citing works
Sealing holes in cellular membranes
Zhen, Y., Radulovic, M., Vietri, M., & Stenmark, H. (2021) · The EMBO Journal · doi:10.15252/embj.2020106922 · Cited by 121 · see citing works
Self-citationBacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily
Liu, J., Tassinari, M., de Souza, D. P., Naskar, S., Noel, J. K., Bohuszewicz, O., Buck, M., Williams, T. A., Baum, B., & Low, H. H. (2021) · Cell · doi:10.1016/j.cell.2021.05.041 · Cited by 114 · see citing works
Plant pathogens convergently evolved to counteract redundant nodes of an NLR immune receptor network
Derevnina, L., Contreras, M. P., Adachi, H., Upson, J., Cruces, A. V., Xie, R., Sklenář, J., Menke, F. L. H., Mugford, S. T., MacLean, D., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001136 · Cited by 119 · see citing works
Endosomal membrane tension regulates ESCRT-III-dependent intra-lumenal vesicle formation
Mercier, V., Larios, J., Molinard, G., Goujon, A., Matile, S., Gruenberg, J. E., & Roux, A. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0546-4 · Cited by 118 · see citing works
Matsui, T., Hiragi, S., Osaki, F., Sakamaki, Y., & Fukuda, M. (2021) · EMBO Reports · doi:10.15252/embr.202051475 · Cited by 112 · see citing works
Molecular Determinants of Flavivirus Virion Assembly
Barnard, T. R., Abram, Q. H., Lin, Q. F., Wang, A. B., & Sagan, S. M. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.007 · Cited by 107 · see citing works
Liu, P., Zhang, Z., & Yao, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.603416 · Cited by 110 · see citing works
Intratumoral heterogeneity and drug resistance in cancer
Fu, Y.-C., Liang, S.-B., Luo, M., & Wang, X. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03734-w · Cited by 121 · see citing works
Extracellular signals regulate the biogenesis of extracellular vesicles
Jin, Y., Ma, L., Zhang, W., Yang, W., Feng, Q., & Wang, H. (2022) · Biological Research · doi:10.1186/s40659-022-00405-2 · Cited by 115 · see citing works
Asleh, K., Dery, V., Taylor, C., Davey, M., Djeungoue‐Petga, M., & Ouellette, R. J. (2023) · Biomarker Research · doi:10.1186/s40364-023-00540-2 · Cited by 107 · see citing works
ESCRT-III-mediated membrane repair in cell death and tumor resistance
Liu, J., Kang, R., & Tang, D. (2020) · Cancer Gene Therapy · doi:10.1038/s41417-020-0200-0 · Cited by 107 · see citing works
Emerging Exosomes and Exosomal MiRNAs in Spinal Cord Injury
Feng, J., Zhang, Y., Zhu, Z., Gu, C., Waqas, A., & Chen, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.703989 · Cited by 106 · see citing works
Extracellular Vesicles for Clinical Diagnostics: From Bulk Measurements to Single-Vesicle Analysis
Tran, H. L., Zheng, W., Issadore, D., Im, H., Cho, Y., Zhang, Y., Liu, D., Liu, Y., Li, B., Liu, F., et al. (2025) · ACS Nano · doi:10.1021/acsnano.5c00706 · Cited by 106 · see citing works
Liu, J., Cvirkaitė‐Krupovič, V., Commère, P., Yang, Y., Zhou, F., Forterre, P., Shen, Y., & Krupovìč, M. (2021) · The ISME Journal · doi:10.1038/s41396-021-00984-0 · Cited by 99 · see citing works
The role and applications of extracellular vesicles in osteoporosis
Fang, F., Yang, J., Wang, J., Li, T., Wang, E., Zhang, D., Liu, X., & Zhou, C. (2024) · Bone Research · doi:10.1038/s41413-023-00313-5 · Cited by 104 · see citing works
Omo‐Lamai, S., Wang, Y., Patel, M. N., Milosavljevic, A., Zuschlag, D. W., Poddar, S., Wu, J., Wang, L., Dong, F., Espy, C. L., et al. (2025) · Nature Nanotechnology · doi:10.1038/s41565-025-01974-5 · Cited by 162 · see citing works
Fang, Y., Wang, Z., Liu, X., & Tyler, B. M. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.817844 · Cited by 99 · see citing works
Shafiei, M., Ansari, M. N. M., Razak, S. I. A., & Khan, M. U. A. (2021) · Polymers · doi:10.3390/polym13152529 · Cited by 100 · see citing works
Nanoparticle entry into cells; the cell biology weak link
Griffiths, G. W., Gruenberg, J. E., Marsh, M., Wohlmann, J., Jones, A. T., & Parton, R. G. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114403 · Cited by 99 · see citing works
Extracellular Vesicles and Viruses: Two Intertwined Entities
Moulin, C., Crupi, M. J. F., Ilkow, C. S., Bell, J. C., & Boulton, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021036 · Cited by 91 · see citing works
The Role of Exosome and the ESCRT Pathway on Enveloped Virus Infection
Ju, Y., Bai, H., Ren, L., & Zhang, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169060 · Cited by 88 · see citing works
Accessory ESCRT‐III proteins are conserved and selective regulators of Rab11a‐exosome formation
Marie, P. P., Fan, S., Mason, J. D., Wells, A., Mendes, C. C., Wainwright, S. M., Scott, S., Fischer, R., Harris, A. L., WILSON, C. G., et al. (2023) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12311 · Cited by 88 · see citing works
Lysosomal quality control: molecular mechanisms and therapeutic implications
Yang, H., & Tan, J. X. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.01.001 · Cited by 84 · see citing works
Termination of STING responses is mediated via ESCRT‐dependent degradation
Balka, K. R., Venkatraman, R., Saunders, T. L., Shoppee, A., Pang, E. S., Magill, Z., Homman‐Ludiye, J., Huang, C., Lane, R. M., York, H. M., et al. (2023) · The EMBO Journal · doi:10.15252/embj.2022112712 · Cited by 87 · see citing works
Principles of membrane remodeling by dynamic ESCRT-III polymers
Pfitzner, A.-K., von Filseck, J. M., & Roux, A. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.04.005 · Cited by 86 · see citing works
Guan, L., Wu, B., Li, T., Beer, L. A., Sharma, G., Li, M., Lee, C. N., Liu, S., Yang, C., Huang, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31713-6 · Cited by 86 · see citing works
Lysosomal microautophagy: an emerging dimension in mammalian autophagy
Kuchitsu, Y., & Taguchi, T. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.11.005 · Cited by 84 · see citing works
The ESCRTs – converging on mechanism
Pavlin, M. R., & Hurley, J. H. (2020) · Journal of Cell Science · doi:10.1242/jcs.240333 · Cited by 83 · see citing works
Overcoming the blood-brain barrier: Exosomes as theranostic nanocarriers for precision neuroimaging
Li, C., Qin, S., Wen, Y., Zhao, W. G., Huang, Y., & Liu, J. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.08.002 · Cited by 85 · see citing works
Recognising the signals for endosomal trafficking
Weeratunga, S. K., Paul, B., & Collins, B. M. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.02.005 · Cited by 82 · see citing works
Wang, X., Xu, P., Bentley‐DeSousa, A., Hancock-Cerutti, W. F., Cai, S., Johnson, B., Tonelli, F., Shao, L., Talaia, G., Alessi, D. R., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01653-6 · Cited by 81 · see citing works
Endocytosis blocks the vesicular secretion of exosome marker proteins
Ai, Y., Guo, C., García-Contreras, M., B., L. S. S., Saftics, A., Shodubi, O., Raghunandan, S., Xu, J., Tsai, S. J., Dong, Y. W., et al. (2024) · Science Advances · doi:10.1126/sciadv.adi9156 · Cited by 80 · see citing works
Blebbisomes are large, organelle-rich extracellular vesicles with cell-like properties
Jeppesen, D. K., Sanchez, Z., Kelley, N. M., Hayes, J. B., Ambroise, J., Koory, E., Krystofiak, E., Taneja, N., Zhang, Q., Dungan, M. M., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01621-0 · Cited by 80 · see citing works
Lysosomal retargeting of Myoferlin mitigates membrane stress to enable pancreatic cancer growth
Gupta, S., Yano, J., Mercier, V., Htwe, H. H., Shin, H. R., Rademaker, G., Cakir, Z., Ituarte, T., Wen, K. W., Kim, G., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00644-7 · Cited by 79 · see citing works
Biomimetic Exosomes: A New Generation of Drug Delivery System
Wang, X., Zhao, X., Zhong, Y., Shen, J., & An, W. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.865682 · Cited by 79 · see citing works
Tau fibrils induce nanoscale membrane damage and nucleate cytosolic tau at lysosomes
Rose, K. M., Jepson, T. A., Shukla, S., Maya-Romero, A., Kampmann, M., Xu, K., & Hurley, J. H. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315690121 · Cited by 79 · see citing works
Hunt, L. C., Schadeberg, B., Stover, J., Haugen, B., Pagala, V., Wang, Y., Puglise, J. M., Barton, E. R., Peng, J., & Demontis, F. (2021) · Nature Communications · doi:10.1038/s41467-021-21738-8 · Cited by 76 · see citing works
Exosomal cargos-mediated metabolic reprogramming in tumor microenvironment
Tan, S., Yang, Y., Yang, W., Han, Y., Huang, L., Yang, R., Hu, Z., Tao, Y., Liu, L., Li, Y., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02634-z · Cited by 79 · see citing works
Native and Bioengineered Exosomes for Ischemic Stroke Therapy
Khan, H. L., Pan, J., Li, Y.-F., Zhang, Z., & Yang, G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.619565 · Cited by 79 · see citing works
Human Milk Extracellular Vesicles: A Biological System with Clinical Implications
Chutipongtanate, S., Morrow, A. L., & Newburg, D. S. (2022) · Cells · doi:10.3390/cells11152345 · Cited by 77 · see citing works
Built to last: lysosome remodeling and repair in health and disease
Zoncu, R., & Perera, R. M. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.12.009 · Cited by 75 · see citing works
The Endo-Lysosomal Damage Response
Meyer, H. H., & Kravić, B. (2024) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030222-102505 · Cited by 76 · see citing works
Microglia as hunters or gatherers of brain synapses
Pereira‐Iglesias, M., Maldonado-Teixidó, J., Melero, A., Piriz, J., Galea, E., Ransohoff, R. M., & Sierra, A. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01818-w · Cited by 81 · see citing works
The Therapeutic Potential of Exosomes in Soft Tissue Repair and Regeneration
Wan, R., Hussain, A., Behfar, A., Moran, S. L., & Zhao, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073869 · Cited by 75 · see citing works
The ESCRT Machinery: Remodeling, Repairing, and Sealing Membranes
Olmos, Y. (2022) · Membranes · doi:10.3390/membranes12060633 · Cited by 69 · see citing works
Peng, Y., Yang, Y., Li, Y., Shi, T., Luan, Y., & Yin, C. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1154217 · Cited by 74 · see citing works
From Exosome Biogenesis to Absorption: Key Takeaways for Cancer Research
Lau, N. C. H., & Yam, J. W. P. (2023) · Cancers · doi:10.3390/cancers15071992 · Cited by 73 · see citing works
Role of Extracellular Vesicles in Autoimmune Pathogenesis
Wu, W., Song, S., Zhang, Y., & Li, X. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.579043 · Cited by 72 · see citing works
De Novo VPS4A Mutations Cause Multisystem Disease with Abnormal Neurodevelopment
Rodger, C. E., Flex, E., Allison, R. J., Sanchis‐Juan, A., Hasenahuer, M. A., Cecchetti, S., French, C. E., Edgar, J. R., Carpentieri, G., Ciolfi, A., et al. (2020) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2020.10.012 · Cited by 69 · see citing works
Structure, biogenesis, and evolution of thylakoid membranes
Ostermeier, M., Garibay‐Hernández, A., Holzer, V. J. C., Schroda, M., & Nickelsen, J. (2024) · The Plant Cell · doi:10.1093/plcell/koae102 · Cited by 70 · see citing works
Zhen, Y., & Stenmark, H. (2023) · Cells · doi:10.3390/cells12040668 · Cited by 65 · see citing works
Self-citationExosomal Non-coding RNAs-Mediated Crosstalk in the Tumor Microenvironment
Chen, Q., Li, Y.-F., Liu, Y.-Q., Xu, W.-L., & Zhu, X.-L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.646864 · Cited by 55 · see citing works
Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage
Azad, K., Guilligay, D., Boscheron, C., Maity, S., Franceschi, N. D., Sulbarán, G., Effantin, G., Wang, H., Kleman, J.-P., Bassereau, P. M., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00867-8 · Cited by 65 · see citing works
de Oliveira, R. C., Tye, G. L., Sampaio, L. P., Shiju, T. M., DeDreu, J., Menko, A. S., de Santhiago, M. R., & Wilson, S. E. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108325 · Cited by 64 · see citing works
Neggers, J. E., Paolella, B. R., Asfaw, A., Rothberg, M. V., Skipper, T. A., Yang, A., Kalekar, R. L., Krill-Burger, J. M., Dharia, N. V., Kugener, G., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108493 · Cited by 64 · see citing works
Involvement of the Actin Machinery in Programmed Cell Death
Ren, W., Zhao, W., Cao, L., & Huang, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.634849 · Cited by 64 · see citing works
Cell entry and release of quasi-enveloped human hepatitis viruses
Das, A., Rivera-Serrano, E. E., Yin, X., Walker, C. M., Feng, Z., & Lemon, S. M. (2023) · Nature Reviews Microbiology · doi:10.1038/s41579-023-00889-z · Cited by 64 · see citing works
Insights Into Exosomal Non-Coding RNAs Sorting Mechanism and Clinical Application
Qiu, Y., Li, P., Zhang, Z., & Wu, M. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.664904 · Cited by 63 · see citing works
Shukla, S., Larsen, K. P., Ou, C., Rose, K. M., & Hurley, J. H. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205590119 · Cited by 63 · see citing works
Negative Regulation of FGFR (Fibroblast Growth Factor Receptor) Signaling
Szybowska, P., Kostas, M., Wesche, J., Haugsten, E., & Wiedlocha, A. (2021) · Cells · doi:10.3390/cells10061342 · Cited by 51 · see citing works
Zhang, D. X., Vu, L. T., Ismail, N. N., Le, M. T. N., & Grimson, A. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.01.007 · Cited by 63 · see citing works
- Authors
- Vietri, M., Radulovic, M., & Stenmark, H.
- Affiliations
- Oslo University Hospital (NO)
- Corresponding author
- Stenmark, Harald
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2019-11-08
- Volume
- 21
- Issue
- 1
- Pages
- 25-42
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2985101511
- Cited by
- 962
- References
- 221
- Citations by year
- 2026: 117 · 2025: 159 · 2024: 165 · 2023: 144 · 2022: 150 · 2021: 152 · 2020: 74 · 2019: 1
- FWCI
- 10.94
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- ESCRT, membrane fission, membrane sealing, cytokinesis, endosome maturation, autophagy, membrane repair, viral replication, budding
- MeSH terms
- Spastin, Animals, Cell Membrane, Humans, Neurons, Nuclear Envelope, Phagosomes, Endosomes, Virus Replication, Protein Transport, Cytokinesis, Host-Pathogen Interactions, Exosomes, Endosomal Sorting Complexes Required for Transport
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