The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
Abstract
Selective trafficking of membrane proteins to lysosomes for destruction is required for proper cell signalling and metabolism. Ubiquitylation aids this process by specifying which proteins should be transported to the lysosome lumen by the multivesicular endosome pathway. The endosomal sorting complex required for transport (ESCRT) machinery sorts cargo labelled with ubiquitin into invaginations of endosome membranes. Then, through a highly conserved mechanism also used in cytokinesis and viral budding, it mediates the breaking off of the cargo-containing intraluminal vesicles from the perimeter membrane. The involvement of the ESCRT machinery in suppressing diseases such as cancer, neurodegeneration and infections underscores its importance to the cell.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the endosome, ubiquitinated ENaC is detected and sorted to lysosomes by Hrs.
“In the endosome, ubiquitinated ENaC is detected and sorted to lysosomes by Hrs (hepatocyte growth factor-regulated tyrosine kinase substrate).”
From Ubiquitin-specific Peptidase 8 (USP8) Regulates Endosomal Trafficking of the Epithelial Na+ Channel* (2013) · cites this paper as [19]
Citations
Cites
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347
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
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
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
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
Self-citationGaullier, J.-M., Simonsen, A., D'Arrigo, A., Bremnes, B., Stenmark, H., & Aasland, R. (1998) · Nature · doi:10.1038/28767 · Cited by 553
Self-citationPlasma 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
ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B)
Parkinson, N., Ince, P. G., Smith, M. O., Highley, R., Skibinski, G., Andersen, P. M., Morrison, K. E., Pall, H. S., Hardiman, O., Collinge, J., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000231510.89311.8b · Cited by 395
Flagged first, then by citations
Research works printed but not linked: 91
- Gruenberg, J. & Stenmark, H. The biogenesis of multivesicular endosomes. Nature Rev. Mol. Cell Biol. 5, 317–323 (2004). · DOI
- Katzmann, D. J., Odorizzi, G. & Emr, S. D. Receptor downregulation and multivesicular-body sorting. Nature Rev. Mol. Cell Biol. 3, 893–905 (2002). · DOI · Paper page
- d'Azzo, A., Bongiovanni, A. & Nastasi, T. E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation. Traffic 6, 429–441 (2005). · DOI
- Hicke, L. & Dunn, R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu. Rev. Cell Dev. Biol. 19, 141–172 (2003). · DOI
- Hicke, L. & Riezman, H. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84, 277–287 (1996). · DOI · Paper page
- Galan, J. M., Moreau, V., Andre, B., Volland, C. & Haguenauer-Tsapis, R. Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271, 10946–10952 (1996). · DOI
- Babst, M., Katzmann, D. J., Snyder, W. B., Wendland, B. & Emr, S. D. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell 3, 283–289 (2002). This paper describes the first biochemical and functional characterization of ESCRT-II. · DOI
- Babst, M., Katzmann, D. J., Estepa-Sabal, E. J., Meerloo, T. & Emr, S. D. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev. Cell 3, 271–282 (2002). This is the first biochemical and functional characterization of ESCRT-III, and identification of Vps20–Vps32 and Vps24–Vps2 as subcomplexes of ESCRT-III. · DOI
- Katzmann, D. J., Babst, M. & Emr, S. D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106, 145–155 (2001). This paper coins the ESCRT name and provides the concept of an endosomal machinery that sorts ubiquitylated cargo into MVEs. It describes the first biochemical and functional characterization of ESCRT-I. · DOI
- Bache, K. G., Brech, A., Mehlum, A. & Stenmark, H. Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J. Cell Biol. 162, 435–442 (2003). · DOI
- Katzmann, D. J., Stefan, C. J., Babst, M. & Emr, S. D. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J. Cell Biol. 162, 413–423 (2003). · DOI
- Lu, Q., Hope, L. W., Brasch, M., Reinhard, C. & Cohen, S. N. TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation. Proc. Natl Acad. Sci. USA 100, 7626–7631 (2003). · DOI · Paper page
- Hurley, J. H. ESCRT complexes and the biogenesis of multivesicular bodies. Curr. Opin. Cell Biol. 20, 4–11 (2008). · DOI
- Williams, R. L. & Urbe, S. The emerging shape of the ESCRT machinery. Nature Rev. Mol. Cell Biol. 8, 355–368 (2007). · DOI
- Prag, G. et al. The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting. Dev. Cell 12, 973–986 (2007). · DOI
- Hofmann, K. & Falquet, L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem. Sci. 26, 347–350 (2001). · DOI
- Raiborg, C., Bache, K. G., Mehlum, A., Stang, E. & Stenmark, H. Hrs recruits clathrin to early endosomes. EMBO J. 20, 5008–5021 (2001). · DOI
- McCullough, J. et al. Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery. Curr. Biol. 16, 160–165 (2006). · DOI
- Burd, C. G. & Emr, S. D. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domain. Mol. Cell 2, 157–162 (1998). · DOI
- Raiborg, C. et al. FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. J. Cell Sci. 114, 2255–2263 (2001). · DOI
- Roxrud, I., Raiborg, C., Pedersen, N. M., Stang, E. & Stenmark, H. An endosomally localized isoform of Eps15 interacts with Hrs to mediate degradation of epidermal growth factor receptor. J. Cell Biol. 180, 1205–1218 (2008). · DOI
- Leung, K. F., Dacks, J. B. & Field, M. C. Evolution of the multivesicular body ESCRT machinery; retention across the eukaryotic lineage. Traffic 9, 1698–1716 (2008). · DOI
- Puertollano, R. & Bonifacino, J. S. Interactions of GGA3 with the ubiquitin sorting machinery. Nature Cell Biol. 6, 244–251 (2004). · DOI · Paper page
- Puertollano, R. Interactions of TOM1L1 with the multivesicular body sorting machinery. J. Biol. Chem. 280, 9258–9264 (2005). · DOI
- Seet, L. F., Liu, N., Hanson, B. J. & Hong, W. Endofin recruits TOM1 to endosomes. J. Biol. Chem. 279, 4670–4679 (2004). · DOI
- Stuchell, M.D. et al. The human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 budding. J. Biol. Chem. 279, 36059–36071 (2004). · DOI
- Kostelansky, M. S. et al. Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer. Cell 129, 485–498 (2007). By combining data from several crystallographic studies, this paper describes a model of almost the whole ESCRT-I from yeast. · DOI · Paper page
- Morita, E. et al. Identification of human MVB12 proteins as ESCRT-I subunits that function in HIV budding. Cell Host Microbe 2, 41–53 (2007). · DOI
- Chu, T., Sun, J., Saksena, S. & Emr, S. D. New component of ESCRT-I regulates endosomal sorting complex assembly. J. Cell Biol. 175, 815–823 (2006). · DOI
- Im, Y. J. & Hurley, J. H. Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. Dev. Cell 14, 902–913 (2008). · DOI
- Hierro, A. et al. Structure of the ESCRT-II endosomal trafficking complex. Nature 431, 221–225 (2004). This is the first determination of the core of yeast ESCRT-II, showing that the core consists of eight winged-helix domains and that ESCRT-II consists of one Vps22, one Vps36 and two copies of Vps25. · DOI
- Teo, H., Perisic, O., Gonzalez, B. & Williams, R. L. ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. Dev. Cell 7, 559–569 (2004). · DOI
- Slagsvold, T. et al. Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain. J. Biol. Chem. 280, 19600–19606 (2005). · DOI
- Hirano, S. et al. Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain. Nature Struct. Mol. Biol. 13, 1031–1032 (2006). · DOI
- Alam, S. L. et al. Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain. Nature Struct. Mol. Biol. 13, 1029–1030 (2006). · DOI
- Teo, H. et al. ESCRT-I core and ESCRT-II GLUE domain structures reveal central role for GLUE domain in linking to ESCRT-I and membranes. Cell 125, 99–111 (2006). This paper shows that the GLUE domain of yeast Vps36 binds Vps28 in ESCRT-I and ubiquitin via yeast-specific NZF zinc fingers, and that another face of the GLUE domain binds the endosomal lipid PtdIns(3)P. · DOI · Paper page
- Lata, S. et al. Structural basis for autoinhibition of ESCRT-III CHMP3. J. Mol. Biol. 378, 816–825 (2008). · DOI
- Teis, D., Saksena, S. & Emr, S. D. Ordered assembly of the ESCRT-III complex on endosomes is required to sequester cargo during MVB formation. Dev. Cell 15, 578–589 (2008). On the basis of biochemical studies of intact yeast cells, this paper provides a model for the ordered assembly of ESCRT-III on membranes. · DOI
- Saksena, S., Wahlman, J., Teis, D., Johnson, A. E. & Emr, S. D. Functional reconstitution of ESCRT-III assembly and disassembly. Cell 136, 97–109 (2009). · DOI
- Rue, S. M., Mattei, S., Saksena, S. & Emr, S. D. Novel Ist1–Did2 complex functions at a late step in multivesicular body sorting. Mol. Biol. Cell 19, 475–484 (2008). · DOI
- Raiborg, C. et al. Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nature Cell Biol. 4, 394–398 (2002). This paper shows that Hrs functions in degradative endosomal sorting of ubiquitylated membrane proteins, and that ESCRT-0 is concentrated in restricted microdomains of the endosome membrane. · DOI · Paper page
- Hirano, S. et al. Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting. Nature Struct. Mol. Biol. 13, 272–277 (2006). · DOI
- Fisher, R. D. et al. Structure and ubiquitin binding of the ubiquitin-interacting motif. J. Biol. Chem. 278, 28976–28984 (2003). · DOI
- Haglund, K. et al. Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nature Cell Biol. 5, 461–466 (2003). · DOI · Paper page
- Huang, F., Kirkpatrick, D., Jiang, X., Gygi, S. & Sorkin, A. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 21, 737–748 (2006). · DOI · Paper page
- Umebayashi, K., Stenmark, H. & Yoshimori, T. Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation. Mol. Biol. Cell 19, 3454–3462 (2008). · DOI
- Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C. & Piper, R. C. The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nature Cell Biol. 4, 534–539 (2002). · DOI
- Raiborg, C., Wesche, J., Malerød, L. & Stenmark, H. Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains. J. Cell Sci. 119, 2414–2424 (2006). · DOI
- Sachse, M., Urbe, S., Oorschot, V., Strous, G. J. & Klumperman, J. Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol. Biol. Cell 13, 1313–1328 (2002). · DOI · Paper page
- Komada, M. & Kitamura, N. Growth factor-induced tyrosine phosphorylation of Hrs, a novel 115-kilodalton protein with a structurally conserved putative zinc finger domain. Mol. Cell. Biol. 15, 6213–6221 (1995). · DOI · Paper page
- Takeshita, T. et al. Cloning of a novel signal-transducing adaptor molecule containing an SH3 domain and ITAM. Biochem. Biophys. Res. Commun. 225, 1035–1039 (1996). · DOI
- Polo, S. et al. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451–455 (2002). · DOI · Paper page
- Hoeller, D. et al. Regulation of ubiquitin-binding proteins by monoubiquitination. Nature Cell Biol. 8, 163–169 (2006). · DOI
- Kim, B. Y., Olzmann, J. A., Barsh, G. S., Chin, L. S. & Li, L. Spongiform neurodegeneration-associated E3 ligase mahogunin ubiquitylates TSG101 and regulates endosomal trafficking. Mol. Biol. Cell 18, 1129–1142 (2007). · DOI
- Doyotte, A., Russell, M. R., Hopkins, C. R. & Woodman, P. G. Depletion of TSG101 forms a mammalian “Class E” compartment: a multicisternal early endosome with multiple sorting defects. J. Cell Sci. 118, 3003–3017 (2005). · DOI
- Conner, S. D. & Schmid, S. L. Regulated portals of entry into the cell. Nature 422, 37–44 (2003). · DOI
- Lata, S. et al. Helical structures of ESCRT-III are disassembled by VPS4. Science 321, 1354–1357 (2008). · DOI
- Ghazi-Tabatabai, S. et al. Structure and disassembly of filaments formed by the ESCRT-III subunit Vps24. Structure 16, 1345–1356 (2008). · DOI
- Pons, V. et al. Hrs and SNX3 functions in sorting and membrane invagination within multivesicular bodies. PLoS Biol. 6, e214 (2008). · DOI
- Obita, T. et al. Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4. Nature 449, 735–739 (2007). · DOI
- Samson, R. Y., Obita, T., Freund, S. M., Williams, R. L. & Bell, S. D. A role for the ESCRT system in cell division in Archaea. Science 322, 1710–1713, (2008). This paper shows that ESCRT-III and Vps4 function in cell division in the archaebacterium Sulfolobus acidocaldarius. · DOI
- Spitzer, C. et al. The Arabidopsis elch mutant reveals functions of an ESCRT component in cytokinesis. Development 133, 4679–4689 (2006). This is the first demonstration that ESCRT proteins are involved in cytokinesis. · DOI
- Pineda-Molina, E. et al. The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Traffic 7, 1007–1016 (2006). · DOI
- Martin-Serrano, J. The role of ubiquitin in retroviral egress. Traffic 8, 1297–1303 (2007). · DOI
- Morita, E. & Sundquist, W. I. Retrovirus budding. Annu. Rev. Cell Dev. Biol. 20, 395–425 (2004). · DOI
- Langelier, C. et al. Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release. J. Virol. 80, 9465–9480 (2006). · DOI · Paper page
- Bowers, K. et al. Degradation of endocytosed epidermal growth factor and virally-ubiquitinated MHC class I is independent of mammalian ESCRTII. J. Biol. Chem. 81, 5094–5105 (2005).
- von Schwedler, U. K. et al. The protein network of HIV budding. Cell 114, 701–713 (2003). · DOI
- McCullough, J., Fisher, R. D., Whitby, F. G., Sundquist, W. I. & Hill, C. P. ALIX–CHMP4 interactions in the human ESCRT pathway. Proc. Natl Acad. Sci. USA 105, 7687–7691 (2008). · DOI
- Amerik, A. Y., Nowak, J., Swaminathan, S. & Hochstrasser, M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol. Biol. Cell 11, 3365–3380 (2000). · DOI
- Swaminathan, S., Amerik, A. Y. & Hochstrasser, M. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol. Biol. Cell 10, 2583–2594 (1999). · DOI
- Nikko, E. & Andre, B. Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway. Traffic 8, 566–581 (2007). · DOI
- Row, P. E., Prior, I. A., McCullough, J., Clague, M. J. & Urbe, S. The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J. Biol. Chem. 281, 12618–12624 (2006). · DOI · Paper page
- Mizuno, E., Kobayashi, K., Yamamoto, A., Kitamura, N. & Komada, M. A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes. Traffic 7, 1017–1031 (2006). · DOI
- Komatsu, M. et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441, 880–884 (2006). · DOI · Paper page
- Nixon, R. A. & Cataldo, A. M. Lysosomal system pathways: genes to neurodegeneration in Alzheimer's disease. J. Alzheimers Dis. 9, 277–289 (2006). · DOI
- Bjørkøy, G. et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171, 603–614 (2005). · DOI · Paper page
- Rusten, T. E., Filimonenko, M., Rodahl, L. M., Stenmark, H. & Simonsen, A. ESCRTing autophagic clearance of aggregating proteins. Autophagy 4, 233–236 (2008). · DOI
- Lee, J. A., Beigneux, A., Ahmad, S. T., Young, S. G. & Gao, F. B. ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr. Biol. 17, 1561–1567 (2007). · DOI
- Kim, B. Y. & Akazawa, C. Endosomal trafficking of EGFR regulated by hVps18 via interaction of MVB sorting machinery. Biochem. Biophys. Res. Commun. Advance online publication doi:10.1016/j.bbrc.2007.08.046 (2007). · DOI
- Li, L. & Cohen, S. N. Tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells. Cell 85, 319–329 (1996). · DOI
- Xu, Z., Liang, L., Wang, H., Li, T. & Zhao, M. HCRP1, a novel gene that is downregulated in hepatocellular carcinoma, encodes a growth-inhibitory protein. Biochem. Biophys. Res. Commun. 311, 1057–1066 (2003). · DOI
- Li, J., Belogortseva, N., Porter, D. & Park, M. Chmp1A functions as a novel tumor suppressor gene in human embryonic kidney and ductal pancreatic tumor cells. Cell Cycle 7, 2886–2893 (2008). · DOI
- Krempler, A., Henry, M. D., Triplett, A. A. & Wagner, K. U. Targeted deletion of the Tsg101 gene results in cell cycle arrest at G1/S and p53-independent cell death. J. Biol. Chem. 277, 43216–43223 (2002). · DOI
- Vaccari, T. & Bilder, D. The Drosophila tumor suppressor vps25 prevents nonautonomous overproliferation by regulating Notch trafficking. Dev. Cell 9, 687–698 (2005). · DOI
- Thompson, B. J. et al. Tumor suppressor properties of the ESCRT-II complex component Vps25 in Drosophila . Dev. Cell 9, 711–720 (2005). · DOI
- Moberg, K. H., Schelble, S., Burdick, S. K. & Hariharan, I. K. Mutations in erupted, the Drosophila ortholog of mammalian tumor susceptibility gene 101, elicit non-cell-autonomous overgrowth. Dev. Cell 9, 699–710 (2005). · DOI
- Philips, J. A., Porto, M. C., Wang, H., Rubin, E. J. & Perrimon, N. ESCRT factors restrict mycobacterial growth. Proc. Natl Acad. Sci. USA 105, 3070–3075 (2008). · DOI
- Vieira, O. V. et al. Acquisition of Hrs, an essential component of phagosomal maturation, is impaired by mycobacteria. Mol. Cell. Biol. 24, 4593–4604 (2004). · DOI
- Singh, S. B., Davis, A. S., Taylor, G. A. & Deretic, V. Human IRGM induces autophagy to eliminate intracellular mycobacteria. Science 313, 1438–1441 (2006). · DOI · Paper page
- Wollert, T., Wunder, C., Lippincott-Schwartz, J. & Hurley, J. H. Membrane scission by the ESCRT-III complex. Nature 458, 159–160 (2009) · DOI
Cited by
Sorted by citations
Extracellular vesicles: Exosomes, microvesicles, and friends
Raposo, G., & Stoorvogel, W. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211138 · Cited by 8,099
Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679
Regulation of immune responses by extracellular vesicles
Robbins, P. D., & Morelli, A. E. (2014) · Nature Reviews Immunology · doi:10.1038/nri3622 · Cited by 2,260
Towards a systems understanding of MHC class I and MHC class II antigen presentation
Neefjes, J., Jongsma, M. L. M., Paul, P., & Bakke, O. (2011) · Nature Reviews Immunology · doi:10.1038/nri3084 · Cited by 2,044
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
Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811
Complex archaea that bridge the gap between prokaryotes and eukaryotes
Spang, A., Saw, J. H., Jørgensen, S. L., Zaremba-Niedzwiedzka, K., Martijn, J., Lind, A. E., van Eijk, R., Schleper, C., Guy, L., & Ettema, T. J. G. (2015) · Nature · doi:10.1038/nature14447 · Cited by 1,324
Asgard archaea illuminate the origin of eukaryotic cellular complexity
Zaremba-Niedzwiedzka, K., Caceres, E. F., Saw, J. H., Bäckström, D., Juzokaite, L., Vancaester, E., Seitz, K. W., Anantharaman, K., Starnawski, P., Kjeldsen, K. U., et al. (2017) · Nature · doi:10.1038/nature21031 · Cited by 1,226
Vietri, M., Radulovic, M., & Stenmark, H. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0177-4 · Cited by 962
Self-citationMolecular mechanism of multivesicular body biogenesis by ESCRT complexes
Wollert, T., & Hurley, J. H. (2010) · Nature · doi:10.1038/nature08849 · Cited by 804
Therapeutically harnessing extracellular vesicles
Cheng, L., & Hill, A. F. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00410-w · Cited by 737
Johnsen, K. B., Gudbergsson, J. M., Skov, M. N., Pilgaard, L., Moos, T., & Duroux, M. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.04.005 · Cited by 704
Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P. (2010) · Autophagy · doi:10.4161/auto.6.2.11014 · Cited by 437
ALIX- and ESCRT-III–dependent sorting of tetraspanins to exosomes
Larios, J., Mercier, V., Roux, A., & Gruenberg, J. (2020) · Journal of Cell Biology · doi:10.1083/jcb.201904113 · Cited by 422
Regulation of exosome production and cargo sorting
Wei, H., Chen, Q., Lin, L., Sha, C., Li, T., Liu, Y., Yin, X., Xu, Y., Chen, L., Gao, W., et al. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.53671 · Cited by 385
Endocytosis and signaling: Cell logistics shape the eukaryotic cell plan
Sigismund, S., Confalonieri, S., Ciliberto, A., Polo, S., Scita, G., & Di Fiore, P. P. (2012) · Physiological Reviews · doi:10.1152/physrev.00005.2011 · Cited by 338
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
Ticket to a bubble ride: Cargo sorting into exosomes and extracellular vesicles
Anand, S., Samuel, M., Kumar, S., & Mathivanan, S. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.02.005 · Cited by 284
Phosphoinositides in Control of Membrane Dynamics
Schink, K. O., Tan, K.-W., & Stenmark, H. (2016) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125349 · Cited by 283
Self-citationESCRT-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
Tau activates microglia via the PQBP1-cGAS-STING pathway to promote brain inflammation
Jin, M., Shiwaku, H., Tanaka, H., Obita, T., Ohuchi, S., Yoshioka, Y., Jin, X., Kondo, K., Fujita, K., Homma, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26851-2 · Cited by 223
Morel, E., Chamoun, Z., Lasiecka, Z. M., Chan, R. B., Williamson, R. L., Vetanovetz, C., Dall’Armi, C., Simoes, S., Point Du Jour, K. S., McCabe, B. D., et al. (2013) · Nature Communications · doi:10.1038/ncomms3250 · Cited by 222
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
Mycobacterium tuberculosis Type VII Secreted Effector EsxH Targets Host ESCRT to Impair Trafficking
Mehra, A., Zahra, A., Thompson, V., Sirisaengtaksin, N., Wells, A., Porto, M., Köster, S., Penberthy, K., Kubota, Y., Dricot, A., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003734 · Cited by 192
MicroRNAs in placental health and disease
Mouillet, J.-F., Ouyang, Y., Coyne, C. B., & Sadovsky, Y. (2015) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2015.05.057 · Cited by 195
Aswad, H., Forterre, A., Wiklander, O. P. B., Vial, G., Danty-Berger, E., Jalabert, A., Lamazière, A., Meugnier, E., Pesenti, S., Ott, C., et al. (2014) · Diabetologia · doi:10.1007/s00125-014-3337-2 · Cited by 185
Zhang, X.-W., Zhou, J.-C., Peng, D., Hua, F., Li, K., Yu, J.-J., Lv, X.-X., Cui, B., Liu, S.-S., Yu, J.-M., et al. (2020) · Autophagy · doi:10.1080/15548627.2019.1635383 · Cited by 166
Atrogin-1 deficiency promotes cardiomyopathy and premature death via impaired autophagy
Zaglia, T., Milan, G., Ruhs, A., Franzoso, M., Bertaggia, E., Pianca, N., Carpi, A., Carullo, P., Pesce, P., Sacerdoti, D., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci66339 · Cited by 147
Berlin, I., Schwartz, H., & Nash, P. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016287 · Cited by 121
Ubiquitin Regulates GGA3-mediated Degradation of BACE1
Kang, E. L., Cameron, A. N., Piazza, F., Walker, K. R., & Tesco, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.092742 · Cited by 111
Azole Drugs Are Imported By Facilitated Diffusion in Candida albicans and Other Pathogenic Fungi
Mansfield, B. E., Oltean, H. N., Oliver, B. G., Hoot, S. J., Leyde, S. E., Hedstrom, L., & White, T. C. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001126 · Cited by 111
Apolipoprotein E4 genotype compromises brain exosome production
Peng, K. Y., Pérez-González, R., Alldred, M. J., Goulbourne, C. N., Morales-Corraliza, J., Saito, M., Saito, M., Ginsberg, S. D., Mathews, P. M., & Levy, E. (2019) · Brain · doi:10.1093/brain/awy289 · Cited by 109
Moorman, N. J., Sharon-Friling, R., Shenk, T., & Cristea, I. M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900485-mcp200 · Cited by 97
NDRG1 functions in LDL receptor trafficking by regulating endosomal recycling and degradation
Pietiäinen, V., Vassilev, B., Blom, T., Wang, W., Nelson, J., Bittman, R., Bäck, N., Zelcer, N., & Ikonen, E. (2013) · Journal of Cell Science · doi:10.1242/jcs.128132 · Cited by 89
ESCRT proteins restrict constitutive NF-κB signaling by trafficking cytokine receptors
Mamińska, A., Bartosik, A., Banach-Orłowska, M., Pilecka, I., Jastrzębski, K., Zdżalik-Bielecka, D., Castanon, I., Poulain, M., Neyen, C., Wolińska-Nizioł, L., et al. (2016) · Science Signaling · doi:10.1126/scisignal.aad0848 · Cited by 74
Self-citationUbiquitin conjugation to Gag is essential for ESCRT-mediated HIV-1 budding
Sette, P., Nagashima, K., Piper, R. C., & Bouamr, F. (2013) · Retrovirology · doi:10.1186/1742-4690-10-79 · Cited by 81
Scotti, E., Calamai, M., Goulbourne, C. N., Zhang, L., Hong, C., Lin, R. R., Choi, J., Pilch, P. F., Fong, L. G., Zou, P., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01716-12 · Cited by 81
Extracellular vesicles in renal tissue damage and regeneration
Bruno, S., Porta, S., & Bussolati, B. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.06.058 · Cited by 74
Sorrentino, V., Nelson, J. K., Maspero, E., Marques, A. R. A., Scheer, L., Polo, S., & Zelcer, N. (2013) · Journal of Lipid Research · doi:10.1194/jlr.m037713 · Cited by 68
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
Self-citationUbiquitin-specific Peptidase 8 (USP8) Regulates Endosomal Trafficking of the Epithelial Na+ Channel*
Zhou, R., Tomkovicz, V. R., Butler, P. L., Ochoa, L. A., Peterson, Z. J., & Snyder, P. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.425272 · Cited by 47
The Dichotomous Role of Extracellular Vesicles in the Central Nervous System
Graykowski, D. R., Wang, Y.-Z., Upadhyay, A., & Savas, J. N. (2020) · iScience · doi:10.1016/j.isci.2020.101456 · Cited by 39
The needs of a synapse—How local organelles serve synaptic proteostasis
Grochowska, K. M., Andres‐Alonso, M., Karpova, A., & Kreutz, M. R. (2022) · The EMBO Journal · doi:10.15252/embj.2021110057 · Cited by 38
Importance of viral late domains in budding and release of enveloped RNA viruses
Welker, L., Paillart, J.-C., & Bernacchi, S. (2021) · Viruses · doi:10.3390/v13081559 · Cited by 36
Metadata
- Authors
- Raiborg, C., & Stenmark, H.
- Venue
- Nature
- Published
- 2009-03-25
- Volume
- 458
- Issue
- 7237
- Pages
- 445-452
- ISSN
- 0028-0836
- 1476-4687
- Cited by
- 1,359
- References
- 9
- Language
- en
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review