Spoiled for Choice: Diverse Endocytic Pathways Function at the Cell Surface
Open accessAbstract
Endocytosis has long been identified as a key cellular process involved in bringing in nutrients, in clearing cellular debris in tissue, in the regulation of signaling, and in maintaining cell membrane compositional homeostasis. While clathrin-mediated endocytosis has been most extensively studied, a number of clathrin-independent endocytic pathways are continuing to be delineated. Here we provide a current survey of the different types of endocytic pathways available at the cell surface and discuss a new classification and plausible molecular mechanisms for some of the less characterized pathways. Along with an evolutionary perspective of the origins of some of these pathways, we provide an appreciation of the distinct roles that these pathways play in various aspects of cellular physiology, including the control of signaling and membrane tension.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Given the physiological size of melanosomes (0.3-0.5 μm in diameter), only macropinocytosis and phagocytosis are predicted to allow internalization of such large cargo.
“Given the physiological size of melanosomes (0.3–0.5 μm in diameter), only macropinocytosis and phagocytosis are predicted to allow the internalization of such large cargo [ 51 , 52 , 53 , 54 ].”
From Melanin's Journey from Melanocytes to Keratinocytes: Uncovering the Molecular Mechanisms of Melanin Transfer and Processing (2023) · cites this paper as [54]
The review’s Macropinocytosis and Phagocytosis subsections (page not provided) describe large macropinocytic vesicles and engulfment of microorganisms, both involving sizes greater than 0.5 μm. They do not give the 0.3–0.5 μm size of melanosomes or say that only these two pathways could internalize them. (LLM, conf=0.84)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929 · see citing works
Regulated portals of entry into the cell
Conner, S. D., & Schmid, S. L. (2003) · Nature · doi:10.1038/nature01451 · Cited by 3,816 · see citing works
Doherty, G. J., & McMahon, H. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081307.110540 · Cited by 3,075 · see citing works
Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790 · see citing works
Huotari, J., & Helenius, A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.286 · Cited by 2,279 · see citing works
Caveolin, a protein component of caveolae membrane coats
Rothberg, K. G., Heuser, J. E., Donzell, W. C., Ying, Y., Glenney, J. R., & Anderson, R. G. W. (1992) · Cell · doi:10.1016/0092-8674(92)90143-z · Cited by 2,259 · see citing works
Molecular mechanism and physiological functions of clathrin-mediated endocytosis
McMahon, H. T., & Boucrot, E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3151 · Cited by 2,223 · see citing works
Maxfield, F. R., & McGraw, T. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1315 · Cited by 1,716 · see citing works
Mechanisms of clathrin-mediated endocytosis
Kaksonen, M., & Roux, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.132 · Cited by 1,698 · see citing works
Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells
Commisso, C., Davidson, S. M., Soydaner-Azeloglu, R. G., Parker, S. J., Kamphorst, J. J., Hackett, S., Grabocka, E., Nofal, M., Drebin, J. A., Thompson, C. B., et al. (2013) · Nature · doi:10.1038/nature12138 · Cited by 1,683 · see citing works
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638 · see citing works
Pathways of clathrin-independent endocytosis
Mayor, S., & Pagano, R. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2216 · Cited by 1,556 · see citing works
Self-citationPathways and mechanisms of endocytic recycling
Grant, B. D., & Donaldson, J. G. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2755 · Cited by 1,468 · see citing works
YOLK PROTEIN UPTAKE IN THE OOCYTE OF THE MOSQUITO AEDES AEGYPTI. L
Roth, T. F., & Porter, K. R. (1964) · The Journal of Cell Biology · doi:10.1083/jcb.20.2.313 · Cited by 1,320 · see citing works
Induction of mutant dynamin specifically blocks endocytic coated vesicle formation.
Damke, H., Baba, T., Warnock, D. E., & Schmid, S. L. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.4.915 · Cited by 1,203 · see citing works
Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
Guglielmo, G. M. D., Roy, C. L., Goodfellow, A. F., & Wrana, J. L. (2003) · Nature Cell Biology · doi:10.1038/ncb975 · Cited by 1,152 · see citing works
EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
Simonsen, A., Lippe, R., Christoforidis, S., Gaullier, J.-M., Brech, A., Callaghan, J., Toh, B.-H., Murphy, C., Zerial, M., & Stenmark, H. (1998) · Nature · doi:10.1038/28879 · Cited by 1,133 · see citing works
The Cell Biology of Phagocytosis
Flannagan, R. S., Jaumouillé, V., & Grinstein, S. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132445 · Cited by 1,018 · see citing works
Rodal, S. K., Skretting, G., Garred, Ø., Vilhardt, F., van Deurs, B., & Sandvig, K. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.4.961 · Cited by 1,009 · see citing works
Cells Respond to Mechanical Stress by Rapid Disassembly of Caveolae
Sinha, B., Köster, D. V., Ruez, R., Gonnord, P., Bastiani, M., Abankwa, D., Stan, R. V., Butler-Browne, G. S., Vedie, B., Johannes, L., et al. (2011) · Cell · doi:10.1016/j.cell.2010.12.031 · Cited by 973 · see citing works
Caveolae as plasma membrane sensors, protectors and organizers
Parton, R. G., & del Pozo, M. Á. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3512 · Cited by 928 · see citing works
Phagocytosis: An Immunobiologic Process
Gordon, S. (2016) · Immunity · doi:10.1016/j.immuni.2016.02.026 · Cited by 902 · see citing works
Kamphorst, J. J., Nofal, M., Commisso, C., Hackett, S. R., Lu, W., Grabocka, E., Vander Heiden, M. G., Miller, G., Drebin, J. A., Bar-Sagi, D., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2211 · Cited by 893 · see citing works
Polarization of Chemoattractant Receptor Signaling During Neutrophil Chemotaxis
Servant, G., Weiner, O. D., Herzmark, P., Balla, T., Sedat, J. W., & Bourne, H. R. (2000) · Science · doi:10.1126/science.287.5455.1037 · Cited by 878 · see citing works
Koivusalo, M., Welch, C. M., Hayashi, H., Scott, C. C., Kim, M., Alexander, T. R., Touret, N., Hahn, K. M., & Grinstein, S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200908086 · Cited by 878 · see citing works
Clathrin-independent endocytosis of ubiquitinated cargos
Sigismund, S., Woelk, T., Puri, C., Maspero, E., Tacchetti, C., Transidico, P., Fiore, P. P. D., & Polo, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409817102 · Cited by 830 · see citing works
THE FINE STRUCTURE OF THE GALL BLADDER EPITHELIUM OF THE MOUSE
Yamada, E. (1955) · The Journal of Cell Biology · doi:10.1083/jcb.1.5.445 · Cited by 816 · see citing works
CLATHRIN-COATED VESICLE FORMATION AND PROTEIN SORTING: An Integrated Process
Schmid, S. L. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.511 · Cited by 800 · see citing works
Honda, A., Nogami, M., Yokozeki, T., Yamazaki, M., Nakamura, H., Watanabe, H., Kawamoto, K., Nakayama, K., Morris, A. J., Frohman, M. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)81540-8 · Cited by 798 · see citing works
Dynamin-mediated Internalization of Caveolae
Henley, J. R., Krueger, E. W. A., Oswald, B. J., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.1.85 · Cited by 767 · see citing works
A High Precision Survey of the Molecular Dynamics of Mammalian Clathrin-Mediated Endocytosis
Taylor, M. J., Perrais, D., & Merrifield, C. J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000604 · Cited by 754 · see citing works
Spatial and Temporal Regulation of 3-Phosphoinositides by PI 3-Kinase and PTEN Mediates Chemotaxis
Funamoto, S., Meili, R., Lee, S. D., Parry, L. A., & Firtel, R. (2002) · Cell · doi:10.1016/s0092-8674(02)00755-9 · Cited by 746 · see citing works
Adaptable adaptors for coated vesicles.
Robinson, M. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.02.002 · Cited by 741 · see citing works
PTRF-Cavin, a conserved cytoplasmic protein required for caveola formation and function.
Hill, M., Bastiani, M., Luetterforst, R., Kirkham, M., Kirkham, A., Nixon, S. J., Walser, P., Abankwa, D., Oorschot, V., Martin, S., et al. (2008) · Cell · doi:10.1016/j.cell.2007.11.042 · Cited by 739 · see citing works
Tang, Z., Scherer, P. E., Okamoto, T., Song, K. S., Chu, C., Kohtz, D. S., Nishimoto, I., Lodish, H. F., & Lisanti, M. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.4.2255 · Cited by 738 · see citing works
Bar-Sagi, D., & Feramisco, J. R. (1986) · Science · doi:10.1126/science.3090687 · Cited by 734 · see citing works
A Modular Design for the Clathrin- and Actin-Mediated Endocytosis Machinery
Kaksonen, M., Toret, C. P., & Drubin, D. G. (2005) · Cell · doi:10.1016/j.cell.2005.09.024 · Cited by 726 · cited 1× · see citing works
“Clathrinrecruitment precedes actin and is postulated to aid in the initial assembly of actin (Kaksonen et al. 2005).”
Receptor-mediated endocytosis: insights from the lipoprotein receptor system.
Brown, M. S., & Goldstein, J. L. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.7.3330 · Cited by 711 · see citing works
Anderson, R. G. W., Brown, M. S., & Goldstein, J. L. (1977) · Cell · doi:10.1016/0092-8674(77)90022-8 · Cited by 698 · see citing works
Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles.
Pearse, B. M. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.4.1255 · Cited by 683 · see citing works
Sigismund, S., Argenzio, E., Tosoni, D., Cavallaro, E. C., Polo, S., & Fiore, P. P. D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.06.012 · Cited by 679 · see citing works
Sabharanjak, S., Sharma, P., Parton, R. G., & Mayor, S. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00145-4 · Cited by 647 · see citing works
Self-citationMechanism of N-Wasp Activation by Cdc42 and Phosphatidylinositol 4,5-Bisphosphate
Rohatgi, R., Ho, H. H., & Kirschner, M. W. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1299 · Cited by 646 · see citing works
A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
Polo, S., Sigismund, S., Faretta, M., Guidi, M., Capua, M. R., Bossi, G., Chen, H., Camilli, P. V. D., & Fiore, P. P. D. (2002) · Nature · doi:10.1038/416451a · Cited by 633 · see citing works
Regulation 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
Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
Glebov, O., Bright, N. A., & Nichols, B. (2006) · Nature Cell Biology · doi:10.1038/ncb1342 · Cited by 609 · see citing works
Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
Pelkmans, L., Fava, E., Grabner, H., Hannus, M., Habermann, B. H., Krausz, E., & Zerial, M. (2005) · Nature · doi:10.1038/nature03571 · Cited by 607 · see citing works
Lipid Rafts and Caveolae as Portals for Endocytosis: New Insights and Common Mechanisms
Parton, R. G., & Richards, A. A. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.00128.x · Cited by 603 · see citing works
To degrade or not to degrade: Mechanisms and significance of endocytic recycling
Cullen, P. J., & Steinberg, F. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0053-7 · Cited by 590 · see citing works
Rab Proteins and the Compartmentalization of the Endosomal System
Wandinger-Ness, A., & Zerial, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022616 · Cited by 586 · see citing works
Acute cholesterol depletion inhibits clathrin-coated pit budding
Subtil, A., Gaidarov, I., Kobylarz, K. A., Lampson, M. A., Keen, J. H., & McGraw, T. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6775 · Cited by 577 · see citing works
Use the force: membrane tension as an organizer of cell shape and motility
Diz-Muñoz, A., Fletcher, D. A., & Weiner, O. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.09.006 · Cited by 574 · see citing works
Coated vesicles from pig brain: Purification and biochemical characterization
Pearse, B. M. F. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80024-6 · Cited by 573 · see citing works
Houk, A. R., Jilkine, A., Mejean, C. O., Boltyanskiy, R., Dufresne, E. R., Angenent, S., Altschuler, S. J., Wu, L. F., & Weiner, O. D. (2012) · Cell · doi:10.1016/j.cell.2011.10.050 · Cited by 567 · see citing works
Identification, sequence, and expression of caveolin-2 defines a caveolin gene family.
Scherer, P. E., Okamoto, T., Ma, C., Nishimoto, I., Lodish, H. F., & Lisanti, M. P. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.131 · Cited by 561 · see citing works
Actin dynamics counteract membrane tension during clathrin-mediated endocytosis
Boulant, S., Kural, C., Zeeh, J., Ubelmann, F., & Kirchhausen, T. L. (2011) · Nature Cell Biology · doi:10.1038/ncb2307 · Cited by 547 · see citing works
Endophilin marks and controls a clathrin-independent endocytic pathway
Boucrot, E., Ferreira, A. P. A., Almeida-Souza, L., Debard, S., Vallis, Y., Howard, G., Bertot, L., Sauvonnet, N., & McMahon, H. T. (2015) · Nature · doi:10.1038/nature14067 · Cited by 542 · see citing works
Integrins Regulate Rac Targeting by Internalization of Membrane Domains
del Pozo, M. Á., Alderson, N. B., Kiosses, W. B., Chiang, H.-H., Anderson, R. G. W., & Schwartz, M. A. (2004) · Science · doi:10.1126/science.1092571 · Cited by 538 · see citing works
Organelle identity and the signposts for membrane traffic
Behnia, R., & Munro, S. (2005) · Nature · doi:10.1038/nature04397 · Cited by 525 · see citing works
Clathrin-independent pathways of endocytosis
Mayor, S., Parton, R. G., & Donaldson, J. G. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016758 · Cited by 525 · see citing works
Self-citationLamaze, C., Dujeancourt-Henry, A., Baba, T., Lo, C. G., Benmerah, A., & Dautry‐Varsat, A. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00212-x · Cited by 525 · see citing works
ADP-Ribosylation Factor 6 Regulates a Novel Plasma Membrane Recycling Pathway
Radhakrishna, H., & Donaldson, J. G. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.1.49 · Cited by 509 · see citing works
Kwik, J. F., Boyle, S., Fooksman, D., Margolis, L. B., Sheetz, M. P., & Edidin, M. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2336102100 · Cited by 485 · see citing works
Molecular structure, function, and dynamics of clathrin-mediated membrane traffic.Preprint
Kirchhausen, T., Owen, D., & Harrison, S. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016725 · Cited by 479 · see citing works
Endocytosis of Receptor Tyrosine KinasesPreprint
Goh, L. K., & Sorkin, A. D. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a017459 · Cited by 462 · see citing works
Dynamin and β-Arrestin Reveal Distinct Mechanisms for G Protein-coupled Receptor Internalization
Zhang, J., Ferguson, S. S. G., Barak, L. S., Ménard, L., & Caron, M. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18302 · Cited by 459 · see citing works
West, M. A. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.6.2731 · Cited by 451 · see citing works
Scita, G., & Fiore, P. P. D. (2010) · Nature · doi:10.1038/nature08910 · Cited by 451 · see citing works
Systems survey of endocytosis by multiparametric image analysis
Collinet, C., Stöter, M., Bradshaw, C. R., Samusik, N., Rink, J. C., Kenski, D. M., Habermann, B. H., Buchholz, F., Henschel, R., Mueller, M., et al. (2010) · Nature · doi:10.1038/nature08779 · Cited by 446 · see citing works
Shpetner, H. S., & Vallee, R. B. (1989) · Cell · doi:10.1016/0092-8674(89)90027-5 · Cited by 443 · see citing works
Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers
Kirkham, M., & Parton, R. G. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.06.002 · Cited by 437 · see citing works
Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic
Brown, F. D., Rozelle, A. L., Yin, H. L., Balla, T., & Donaldson, J. G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103107 · Cited by 435 · see citing works
Repair of injured plasma membrane by rapid Ca2+-dependent endocytosis
Idone, V. J., Tam, C. C., Goss, J. A., Toomre, D. K., Pypaert, M., & Andrews, N. W. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708010 · Cited by 429 · see citing works
Mechanical feedback between membrane tension and dynamics
Gauthier, N. C., Masters, T. A., & Sheetz, M. P. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2012.07.005 · Cited by 427 · see citing works
Phospho-caveolin-1 mediates integrin-regulated membrane domain internalization
del Pozo, M. Á., Balasubramanian, N., Alderson, N. B., Kiosses, W. B., Grande-García, A., Anderson, R. G. W., & Schwartz, M. A. (2005) · Nature Cell Biology · doi:10.1038/ncb1293 · Cited by 424 · see citing works
Damke, H., Baba, T., van der Bliek, A. M., & Schmid, S. L. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.1.69 · Cited by 410 · see citing works
David, C., McPherson, P. S., Mundigl, O., & Camilli, P. V. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.331 · Cited by 409 · see citing works
Laporte, S. A., Oakley, R. H., Holt, J. A., Barak, L. S., & Caron, M. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002581200 · Cited by 401 · see citing works
Transbilayer Lipid Interactions Mediate Nanoclustering of Lipid-Anchored Proteins
Raghupathy, R., Anilkumar, A. A., Polley, A., Singh, P. P., Yadav, M., Johnson, C., Suryawanshi, S., Saikam, V., Sawant, S. D., Panda, A., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.048 · Cited by 377 · see citing works
Self-citationExocytosis of acid sphingomyelinase by wounded cells promotes endocytosis and plasma membrane repair
Tam, C. C., Idone, V. J., Devlin, C. M., Fernandes, M. C., Flannery, A. R., He, X., Schuchman, E. H., Tabas, I. A., & Andrews, N. W. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201003053 · Cited by 365 · see citing works
Santolini, E., Puri, C., Salcini, A. E., Gagliani, M. C., Pelicci, P. G., Tacchetti, C., & Fiore, P. P. D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.6.1345 · Cited by 363 · see citing works
Forty Years of Clathrin‐coated Vesicles
Robinson, M. S. (2015) · Traffic · doi:10.1111/tra.12335 · Cited by 359 · see citing works
Guglielmo, G. M. D., Baass, P. C., Ou, W. J., Posner, B. I., & Bergeron, J. J. M. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06747.x · Cited by 355 · see citing works
Acidification of the cytosol inhibits endocytosis from coated pits.
Sandvig, K., Olsnes, S., PETERSEN, O. W., & van Deurs, B. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.105.2.679 · Cited by 343 · see citing works
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 · see citing works
Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers
Lakshminarayan, R., Wunder, C., Becken, U., Howes, M. T., Benzing, C., Arumugam, S., Sales, S., Ariotti, N., Chambon, V., Lamaze, C., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb2970 · Cited by 321 · see citing works
Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
Daumke, O., Lundmark, R., Vallis, Y., Martens, S., Butler, P. J. G., & McMahon, H. T. (2007) · Nature · doi:10.1038/nature06173 · Cited by 317 · see citing works
Endophilin-A2 functions in membrane scission in clathrin-independent endocytosis
Renard, H., Simunovic, M., Lemiere, J. P. C., Boucrot, E., Garcia-Castillo, M. D., Arumugam, S., Chambon, V., Lamaze, C., Wunder, C., Kenworthy, A. K., et al. (2014) · Nature · doi:10.1038/nature14064 · Cited by 314 · see citing works
Moya‐Nilges, M., Dautry‐Varsat, A., Goud, B., Louvard, D., & Boquet, P. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.2.548 · Cited by 310 · see citing works
The Fifth Adaptor Protein Complex
Hirst, J., Barlow, L. D., Francisco, G. C., Sahlender, D. A., Seaman, M. N. J., Dacks, J. B., & Robinson, M. S. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001170 · Cited by 307 · see citing works
Kosaka, T., & Ikeda, K. (1983) · Journal of Neurobiology · doi:10.1002/neu.480140305 · Cited by 303 · see citing works
Howes, M. T., Kirkham, M., Riches, J., Cortese, K., Walser, P. J., Simpson, F., Hill, M. M., Jones, A., Lundmark, R., Lindsay, M. R., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201002119 · Cited by 303 · see citing works
Self-citationExploring the caves: cavins, caveolins and caveolae
Hansen, C. G., & Nichols, B. J. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.005 · Cited by 296 · see citing works
Caveolin Is Necessary for Wnt-3a-Dependent Internalization of LRP6 and Accumulation of β-Catenin
Yamamoto, H., Komekado, H., & Kikuchi, A. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.07.003 · Cited by 296 · see citing works
Dynasore - not just a dynamin inhibitor
Preta, G., Cronin, J., & Sheldon, I. M. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0102-1 · Cited by 292 · see citing works
Dynamin 2 Is Required for Phagocytosis in Macrophages
Gold, E. S., Underhill, D. M., Morrissette, N. S., Guo, J., McNiven, M. A., & Aderem, A. A. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.190.12.1849 · Cited by 286 · see citing works
MURC/Cavin-4 and cavin family members form tissue-specific caveolar complexes
Bastiani, M., Liu, L., Hill, M. M. C., Jedrychowski, M. P., Nixon, S. J., Lo, H. P., Abankwa, D., Luetterforst, R., Fernandez-Rojo, M. A., Breen, M. R., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903053 · Cited by 283 · see citing works
Frick, M., Bright, N. A., Riento, K., Bray, A., Merrified, C., & Nichols, B. (2007) · Current Biology · doi:10.1016/j.cub.2007.05.078 · Cited by 283 · see citing works
The Simultaneous Symbiotic Origin of Mitochondria, Chloroplasts, and Microbodies
Cavalier‐Smith, T. (1987) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1987.tb40597.x · Cited by 278 · see citing works
The roles of flotillin microdomains – endocytosis and beyond
Otto, G. P., & Nichols, B. J. (2011) · Journal of Cell Science · doi:10.1242/jcs.092015 · Cited by 278 · see citing works
Anderson, R. G. W., Goldstein, J. L., & Brown, M. S. (1977) · Nature · doi:10.1038/270695a0 · Cited by 274 · see citing works
Modulation of membrane traffic by mechanical stimuli
Apodaca, G. L. (2002) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2002.282.2.f179 · Cited by 273 · see citing works
Endocytic Trafficking of Integrins in Cell Migration
Paul, N. R., Jacquemet, G., & Caswell, P. T. (2015) · Current Biology · doi:10.1016/j.cub.2015.09.049 · Cited by 273 · see citing works
Biogenesis of Caveolae: Stepwise Assembly of Large Caveolin and Cavin Complexes
Hayer, A., Stoeber, M., Bissig, C., & Helenius, A. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.01023.x · Cited by 270 · see citing works
West, M. A., Prescott, A. R., Eskelinen, E., Ridley, A. J., & Watts, C. K. W. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00595-9 · Cited by 268 · see citing works
Hinrichsen, L., Harborth, J., Andrees, L., Weber, K. K., & Ungewickell, E. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307290200 · Cited by 266 · see citing works
IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions
Scita, G., Confalonieri, S., Lappalainen, P., & Suetsugu, S. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.12.002 · Cited by 256 · see citing works
The GTPase-Activating Protein GRAF1 Regulates the CLIC/GEEC Endocytic Pathway
Lundmark, R., Doherty, G. J., Howes, M. T., Cortese, K., Vallis, Y., Parton, R. G., & McMahon, H. T. (2008) · Current Biology · doi:10.1016/j.cub.2008.10.044 · Cited by 253 · see citing works
Life of a clathrin coat: insights from clathrin and AP structures
Edeling, M., Smith, C. J., & Owen, D. J. (2006) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1786 · Cited by 253 · see citing works
Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors
Park, R. J.-H., Shen, H., Liu, L., Liu, X., Ferguson, S. M., & Camilli, P. V. D. (2013) · Journal of Cell Science · doi:10.1242/jcs.138578 · Cited by 249 · see citing works
Actin Dynamics Drive Membrane Reorganization and Scission in Clathrin-Independent Endocytosis
Römer, W., Pontani, L.-L., Sorre, B., Rentero, C., Berland, L., Chambon, V., Lamaze, C., Bassereau, P. M., Sykes, C., Gaus, K., et al. (2010) · Cell · doi:10.1016/j.cell.2010.01.010 · Cited by 248 · see citing works
M‐caveolin, a muscle‐specific caveolin‐related protein
Way, M., & Parton, R. G. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)82884-5 · Cited by 245 · see citing works
Let's go bananas: revisiting the endocytic BAR code
Qualmann, B., Koch, D. C., & Kessels, M. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.266 · Cited by 244 · see citing works
Modulation of membrane dynamics and cell motility by membrane tension
Sheetz, M. P., & Dai, J. (1996) · Trends in Cell Biology · doi:10.1016/0962-8924(96)80993-7 · Cited by 235 · see citing works
Distinct Recycling of Active and Inactive β1 Integrins
Arjonen, A., Alanko, J., Veltel, S., & Ivaska, J. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01327.x · Cited by 227 · see citing works
ARF1 is directly involved in dynamin-independent endocytosis
Kumari, S., & Mayor, S. (2007) · Nature Cell Biology · doi:10.1038/ncb1666 · Cited by 224 · see citing works
Self-citationChadda, R., Howes, M. T., Plowman, S. J., Hancock, J. F., Parton, R. G., & Mayor, S. (2007) · Traffic : the International Journal of Intracellular Transport · doi:10.1111/j.1600-0854.2007.00565.x · Cited by 218 · see citing works
Self-citationFriction Mediates Scission of Tubular Membranes Scaffolded by BAR Proteins
Simunovic, M., Manneville, J., Renard, H., Evergren, E., Raghunathan, K., Bhatia, D. D., Kenworthy, A. K., Voth, G. A., Prost, J., McMahon, H. T., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.047 · Cited by 210 · see citing works
EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization
Morén, B., Shah, C., Howes, M. T., Schieber, N. L., McMahon, H. T., Parton, R. G., Daumke, O., & Lundmark, R. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0787 · Cited by 207 · see citing works
Coated pits act as molecular filters.
Bretscher, M. S., Thomson, J. N., & Pearse, B. M. F. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.7.4156 · Cited by 205 · see citing works
Sphingomyelinase Treatment Induces ATP-independent Endocytosis
Zha, X., Pierini, L. M., Leopold, P. L., Skiba, P. J., Tabas, I. A., & Maxfield, F. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.1.39 · Cited by 201 · see citing works
Building endocytic pits without clathrin
Johannes, L., Parton, R. G., Bassereau, P. M., & Mayor, S. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3968 · Cited by 201 · see citing works
Self-citationClathrin-independent pathways do not contribute significantly to endocytic flux
Bitsikas, V., Corrêa, I. R., & Nichols, B. J. (2014) · eLife · doi:10.7554/elife.03970 · Cited by 199 · see citing works
Kim, S. M., Nguyen, T. T., Ravi, A., Kubiniok, P., Finicle, B. T., Jayashankar, V., Malacrida, L., Hou, J., Robertson, J., Gao, D., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-1215 · Cited by 199 · see citing works
Clathrin-independent endocytosis: an increasing degree of complexity
Sandvig, K., Kavaliauskiene, S., & Skotland, T. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1678-5 · Cited by 196 · see citing works
Phosphoinositide conversion in endocytosis and the endolysosomal system
Wallroth, A., & Haucke, V. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.000629 · Cited by 195 · see citing works
Identification of phagocytosis regulators using magnetic genome-wide CRISPR screens
Haney, M. S., Bohlen, C. J., Morgens, D. W., Ousey, J. A., Barkal, A. A., Tsui, C. K., Ego, B. K., Levin, R., Kamber, R. A., Collins, H., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0254-1 · Cited by 193 · see citing works
The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH
Maurer, M. E., & Cooper, J. A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03217 · Cited by 191 · see citing works
Fujita, A., Cheng, J., Tauchi-Sato, K., Takenawa, T., & Fujimoto, T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900216106 · Cited by 187 · see citing works
Membrane fission by protein crowding
Snead, W. T., Hayden, C. C., Gadok, A. K., Zhao, C., Lafer, E. M., Rangamani, P., & Stachowiak, J. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616199114 · Cited by 177 · see citing works
Endocytic Crosstalk: Cavins, Caveolins, and Caveolae Regulate Clathrin-Independent Endocytosis
Chaudhary, N., Gomez, G. A., Howes, M. T., Lo, H. P., McMahon, K., Rae, J. A., Schieber, N. L., Hill, M. M. C., Gaus, K., Yap, A. S., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001832 · Cited by 175 · see citing works
Oligomers of the ATPase EHD2 confine caveolae to the plasma membrane through association with actin
Stoeber, M., Stoeck, I. K., Hänni, C., Bleck, C. K. E., Balistreri, G., & Helenius, A. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.98 · Cited by 174 · see citing works
Threshold‐controlled ubiquitination of the EGFR directs receptor fate
Sigismund, S., Algisi, V., Nappo, G., Conte, A., Pascolutti, R., Cuomo, A., Bonaldi, T., Argenzio, E., Verhoef, L. G. G. C., Maspero, E., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.149 · Cited by 172 · see citing works
CtBP3/BARS drives membrane fission in dynamin-independent transport pathways
Bonazzi, M., Spanò, S., Turacchio, G., Cericola, C., Valente, C., Colanzi, A., Kweon, H. S., Hsu, V. W., Polishchuck, E. V., Polishchuck, R. S., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1260 · Cited by 171 · see citing works
Endocytosis, Signaling, and BeyondPreprint
Paolo, P., & von Zastrow, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016865 · Cited by 169 · see citing works
Mechanisms of Carrier Formation during Clathrin-Independent Endocytosis
Ferreira, A. P. A., & Boucrot, E. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.11.004 · Cited by 167 · see citing works
Design principles for robust vesiculation in clathrin-mediated endocytosis
Hassinger, J., OSTER, G. F., Drubin, D. G., & Rangamani, P. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617705114 · Cited by 167 · see citing works
Sousa, L. P., Lax, I., Shen, H., Ferguson, S. M., Camilli, P. V. D., & Schlessinger, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200164109 · Cited by 163 · see citing works
Signal processing by the endosomal system
Villaseñor, R., Kalaidzidis, Y. L., & Zerial, M. (2016) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2016.02.002 · Cited by 163 · see citing works
Aboulaich, N., Vainonen, J. P., Strålfors, P., & Vener, A. V. (2004) · Biochemical Journal · doi:10.1042/bj20040647 · Cited by 161 · see citing works
mTORC1 activity repression by late endosomal phosphatidylinositol 3,4-bisphosphate
Marat, A. L., Wallroth, A., Lo, W., Müller, R., Norata, G. D., Falasca, M., Schultz, C., & Haucke, V. (2017) · Science · doi:10.1126/science.aaf8310 · Cited by 160 · see citing works
Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins).
Robinson, M. S. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.3.833 · Cited by 159 · see citing works
Okamoto, Y., Ninomiya, H., Miwa, S., & Masaki, Τ. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6439 · Cited by 156 · see citing works
Thottacherry, J. J., Kosmalska, A. J., Kumar, A., Vishen, A. S., Elósegui-Artola, A., Pradhan, S., Sharma, S., Singh, P. P., Guadamillas, M. C., Chaudhary, N., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06738-5 · Cited by 153 · see citing works
Self-citationProliferation Versus Migration in Platelet-derived Growth Factor Signaling
Donatis, A. D., Comito, G., Buricchi, F., Vinci, M. C., Parenti, A., Caselli, A., Camici, G., Manao, G., Ramponi, G., & Cirri, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709428200 · Cited by 150 · see citing works
Henriksen, L., Grandal, M. V., Knudsen, S. L. J., van Deurs, B., & Grøvdal, L. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058148 · Cited by 148 · see citing works
Segregation of PIP2 and PIP3 into distinct nanoscale regions within the plasma membrane
Wang, J., & Richards, D. A. (2012) · Biology Open · doi:10.1242/bio.20122071 · Cited by 146 · see citing works
Jackson, A. P., Seow, H. F., Holmes, N. J., Drickamer, K., & Parham, P. (1987) · Nature · doi:10.1038/326154a0 · Cited by 145 · see citing works
Fast, Temperature-Sensitive and Clathrin-Independent Endocytosis at Central Synapses
Delvendahl, I., Vyleta, N. P., von Gersdorff, H., & Hallermann, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.013 · Cited by 141 · see citing works
Biophysical approaches to protein-induced membrane deformations in trafficking
Sens, P., Johannes, L., & Bassereau, P. M. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.04.004 · Cited by 140 · see citing works
Phosphoinositide regulation of clathrin-mediated endocytosis
Haucke, V. (2005) · Biochemical Society Transactions · doi:10.1042/bst0331285 · Cited by 140 · see citing works
Physical principles of membrane remodelling during cell mechanoadaptation
Kosmalska, A. J., Casares, L., Elósegui-Artola, A., Thottacherry, J. J., Moreno-Vicente, R., González-Tarragó, V., del Pozo, M. Á., Mayor, S., Arroyo, M., Navajas, D., et al. (2015) · Nature Communications · doi:10.1038/ncomms8292 · Cited by 139 · see citing works
Self-citationMicrotubule-dependent endosomal sorting of clathrin-independent cargo by Hook1
Maldonado‐Báez, L., Cole, N. B., Krämer, H., & Donaldson, J. G. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201208172 · Cited by 132 · see citing works
Krauss, M., Kukhtina, V., Pechstein, A., & Haucke, V. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510306103 · Cited by 129 · see citing works
Bucher, D., Frey, F., Sochacki, K., Kummer, S., Bergeest, J.-P., Godinez, W., Kräusslich, H., Rohr, K., Taraska, J. W., Schwarz, U., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03533-0 · Cited by 128 · see citing works
Phosphoinositide regulation of clathrin-mediated endocytosis
Haucke, V. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051285 · Cited by 127 · see citing works
Dacks, J. B., Poon, P. P., & Field, M. C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707318105 · Cited by 127 · see citing works
Tse, S. M. L., Furuya, W., Gold, E., Schreiber, A. D., Sandvig, K., Inman, R. D., & Grinstein, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207966200 · Cited by 124 · see citing works
Ogata, T., Ueyama, T., Isodono, K., Tagawa, M., Takehara, N., Kawashima, T., Harada, K., Takahashi, T., Shioi, T., Matsubara, H., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02186-07 · Cited by 122 · see citing works
Evolutionary analysis and molecular dissection of caveola biogenesis
Kirkham, M., Nixon, S. J., Howes, M. T., Abi‐Rached, L., Wakeham, D. E., Hanzal‐Bayer, M., Ferguson, C., Hill, M. M. C., Fernandez-Rojo, M. A., Brown, D. A., et al. (2008) · Journal of Cell Science · doi:10.1242/jcs.024588 · Cited by 121 · see citing works
Tubular clathrin/AP-2 lattices pinch collagen fibers to support 3D cell migration
Elkhatib, N., Bresteau, E., Baschieri, F., Rioja, A. L., van Niel, G., Vassilopoulos, S., & Montagnac, G. (2017) · Science · doi:10.1126/science.aal4713 · Cited by 121 · see citing works
Plasma Membrane Area Increases with Spread Area by Exocytosis of a GPI-anchored Protein Compartment
Gauthier, N. C., Rossier, O., Mathur, A., Hone, J., & Sheetz, M. P. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0071 · Cited by 118 · see citing works
Sehat, B., Andersson, S., Girnita, L., & Larsson, O. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6364 · Cited by 116 · see citing works
Membrane Fission: The Biogenesis of Transport Carriers
Campelo, F., & Malhotra, V. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051710-094912 · Cited by 114 · see citing works
Kalia, M., Kumari, S., Chadda, R., Hill, M. M. C., Parton, R. G., & Mayor, S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-10-0980 · Cited by 112 · see citing works
Self-citationClathrin Light Chains LCA and LCB Are Similar, Polymorphic, and Share Repeated Heptad Motifs
Kirchhausen, T. L., Scarmato, P., Harrison, S. C., Monroe, J. J., Chow, E. P., Mattaliano, R. J., Ramachandran, K. L., Smart, J. E., Ahn, A. H., & Brosius, J. (1987) · Science · doi:10.1126/science.3563513 · Cited by 109 · see citing works
High variability of genomic instability and gene expression profiling in different HeLa clones
Frattini, A., Fabbri, M., Valli, R., De Paoli, E., Montalbano, G., Gribaldo, L., Pasquali, F., & Maserati, E. (2015) · Scientific Reports · doi:10.1038/srep15377 · Cited by 109 · see citing works
Rappoport, J. Z., & Simon, S. M. (2009) · Journal of Cell Science · doi:10.1242/jcs.040030 · Cited by 107 · see citing works
Sathe, M., Muthukrishnan, G., Rae, J., Disanza, A., Thattai, M., Scita, G., Parton, R. G., & Mayor, S. (2018) · Nature Communications · doi:10.1038/s41467-018-03955-w · Cited by 107 · see citing works
Self-citationField, M. C., Gabernet‐Castello, C., & Dacks, J. B. (2008) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-74021-8_7 · Cited by 105 · see citing works
Cell Blebbing and Membrane Area Homeostasis in Spreading and Retracting Cells
Norman, L. L., Jan Brugués, A., Sengupta, K., Sens, P., & Aranda‐Espinoza, H. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.07.031 · Cited by 104 · see citing works
Moreau, H. D., Blanch-Mercader, C., Attia, R., Maurin, M., Alraies, Z., Sanséau, D., Malbec, O., Delgado, M., Bousso, P., Joanny, J., et al. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.03.024 · Cited by 102 · see citing works
The Nef Protein of HIV-1 Induces Loss of Cell Surface Costimulatory Molecules CD80 and CD86 in APCs
Chaudhry, A., Das, S. R., Hussain, A., Mayor, S., George, A., Bal, V., Jameel, S., & Rath, S. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.7.4566 · Cited by 97 · see citing works
Self-citationKumari, S., Borroni, V., Chaudhry, A., Chanda, B., Massol, R., Mayor, S., & Barrantes, F. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709086 · Cited by 95 · see citing works
Self-citationAït‐Slimane, T., Galmes, R., Trugnan, G., & Maurice, M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-04-0275 · Cited by 95 · see citing works
Chan Wah Hak, L., Khan, S., Di Meglio, I., Law, A.-L., Lucken-Ardjomande Häsler, S., Quintaneiro, L. M., Ferreira, A. P. A., Krause, M., McMahon, H. T., & Boucrot, E. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0146-8 · Cited by 95 · see citing works
Gaechter, V., Schraner, E. M., Wild, P., & Hehl, A. B. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00657.x · Cited by 93 · see citing works
Chanez, A., Hehl, A. B., Engstler, M., & Schneider, A. (2006) · Journal of Cell Science · doi:10.1242/jcs.03023 · Cited by 93 · see citing works
Clathrin heavy chain: molecular cloning and complete primary structure.
Kirchhausen, T. L., Harrison, S. C., Chow, E. P., Mattaliano, R. J., Ramachandran, K. L., Smart, J. E., & Brosius, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.8805 · Cited by 91 · see citing works
Bairstow, S. F., Ling, K., Su, X., Firestone, A. J., Carbonara, C., & Anderson, R. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601465200 · Cited by 89 · see citing works
Guha, A., Sriram, V., Krishnan, K. S., & Mayor, S. (2003) · Journal of Cell Science · doi:10.1242/jcs.00637 · Cited by 88 · see citing works
Self-citationDelaney, K. A., Murph, M. M., Brown, L. M., & Radhakrishna, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205293200 · Cited by 86 · see citing works
Baral, A., Irani, N. G., Fujimoto, M., Nakano, A., Mayor, S., & Mathew, M. K. (2015) · The Plant Cell · doi:10.1105/tpc.15.00154 · Cited by 85 · see citing works
Self-citationFolate receptors targeted to clathrin-coated pits cannot regulate vitamin uptake.
Ritter, T. E., Fajardo, O., Matsue, H., Anderson, R. G. W., & Lacey, S. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.9.3824 · Cited by 83 · see citing works
Mechanoregulation of clathrin-mediated endocytosis
Ferguson, J. P., Huber, S. D., Willy, N. M., Aygün, E., Goker, S., Atabey, T., & Kural, C. (2017) · Journal of Cell Science · doi:10.1242/jcs.205930 · Cited by 81 · see citing works
Gold, S., Monaghan, P., Mertens, P., & Jackson, T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011360 · Cited by 80 · see citing works
Dynamin‐Actin Cross Talk Contributes to Phagosome Formation and Closure
Marie‐Anaïs, F., Mazzolini, J., Herit, F., & Niedergang, F. (2016) · Traffic · doi:10.1111/tra.12386 · Cited by 78 · see citing works
On the Archaeal Origins of Eukaryotes and the Challenges of Inferring Phenotype from Genotype
Dey, G., Thattai, M., & Baum, B. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.03.009 · Cited by 78 · see citing works
Hilgemann, D. W., Fine, M., Linder, M. E., Jennings, B. C., & Lin, M.-J. (2013) · eLife · doi:10.7554/elife.01293 · Cited by 77 · see citing works
Endocytosis: Past, Present, and FuturePreprint
Schmid, S. L., Sorkin, A. D., & Zerial, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022509 · Cited by 77 · see citing works
Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2
Franceschi, N. D., Arjonen, A., Elkhatib, N., Denessiouk, K. A., Wrobel, A. G., Wilson, T. A., Pouwels, J., Montagnac, G., Owen, D. J., & Ivaska, J. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3161 · Cited by 76 · see citing works
Induced Domain Formation in Endocytic Invagination, Lipid Sorting, and Scission
Johannes, L., & Mayor, S. (2010) · Cell · doi:10.1016/j.cell.2010.08.007 · Cited by 74 · see citing works
Self-citationMURC, a muscle-restricted coiled-coil protein, is involved in the regulation of skeletal myogenesis
Tagawa, M., Ueyama, T., Ogata, T., Takehara, N., Nakajima, N., Isodono, K., Asada, S., Takahashi, T., Matsubara, H., & Oh, H. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00188.2008 · Cited by 74 · see citing works
Gupta, G. D., Swetha, M. G., Kumari, S., Lakshminarayan, R., Dey, G., & Mayor, S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006768 · Cited by 71 · see citing works
Self-citationNeumann, S., & Schmid, S. L. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.490474 · Cited by 69 · see citing works
EGF‐Induced Activation of the EGF Receptor Does Not Trigger Mobilization of Caveolae
Kazazić, M., Roepstorff, K., Johannessen, L. E., Pedersen, N. M., van Deurs, B., Stang, E., & Madshus, I. H. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00487.x · Cited by 69 · see citing works
Compeer, E. B., Kraus, F., Ecker, M., Redpath, G., Amiezer, M., Rother, N., Nicovich, P. R., Kapoor‐Kaushik, N., Deng, Q., Samson, G. P. B., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04088-w · Cited by 69 · see citing works
ATP-dependent membrane remodeling links EHD1 functions to endocytic recycling
Deo, R., Kushwah, M. S., Kamerkar, S. C., Kadam, N. Y., Dar, S., Babu, K., Srivastava, A. K., & Pucadyil, T. J. (2018) · Nature Communications · doi:10.1038/s41467-018-07586-z · Cited by 69 · see citing works
Synaptojanin 2 Functions at an Early Step of Clathrin-Mediated Endocytosis
Rusk, N., Le, P. U., Mariggiò, S., Guay, G., Lurisci, C., Nabi, I. R., Corda, D., & Symons, M. H. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00241-0 · Cited by 68 · see citing works
Ueber die Beziehung der Phagocyten zu Milzbrandbacillen
Metschnikoff, E. (1884) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf02430437 · Cited by 64 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Key principles and methods for studying the endocytosis of biological and nanoparticle therapeutics
Rennick, J. J., Johnston, A. P. R., & Parton, R. G. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-00858-8 · Cited by 1,500 · see citing works
TLR4 and CD14 trafficking and its influence on LPS-induced pro-inflammatory signaling
Ciesielska, A., Matyjek, M., & Kwiatkowska, K. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03656-y · Cited by 1,420 · see citing works
Targeted protein degradation: advances in drug discovery and clinical practice
Zhong, G., Chang, X., Xie, W., & Zhou, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02004-x · Cited by 326 · see citing works
Endocytosis in cancer and cancer therapy
Banushi, B., Joseph, S. R., Lum, B., Lee, J. J., & Simpson, F. (2023) · Nature reviews. Cancer · doi:10.1038/s41568-023-00574-6 · Cited by 245 · see citing works
Gandek, T. B., van der Koog, L., & Nagelkerke, A. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202300319 · Cited by 242 · see citing works
Endocytosis in the context-dependent regulation of individual and collective cell properties
Sigismund, S., Lanzetti, L., Scita, G., & Di Fiore, P. P. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00375-5 · Cited by 132 · see citing works
Endocytosis of abiotic nanomaterials and nanobiovectors: Inhibition of membrane trafficking
Makvandi, P., Chen, M., Sartorius, R., Zarrabi, A., Ashrafizadeh, M., Moghaddam, F. D., Ma, J., Mattoli, V., & Tay, F. R. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101279 · Cited by 129 · see citing works
Endocytosis and Organelle Targeting of Nanomedicines in Cancer Therapy
Wang, X., Qiu, Y., Wang, M., Zhang, C.-H., Zhang, T., Zhou, H., Zhao, W., Zhao, W., Xia, G., & Shao, R. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s274289 · Cited by 126 · see citing works
Molecular mechanism of Fast Endophilin-Mediated Endocytosis
Casamento, A., & Boucrot, E. (2020) · Biochemical Journal · doi:10.1042/bcj20190342 · Cited by 103 · see citing works
Unconventional endocytic mechanisms
Renard, H., & Boucrot, E. (2021) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2021.03.001 · Cited by 102 · see citing works
Nanoparticle entry into cells; the cell biology weak link
Griffiths, G. W., Grüenberg, J., 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
Bento-Lopes, L., Cabaço, L. C., Charneca, J., Neto, M. V., Seabra, M. C., & Barral, D. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411289 · Cited by 114 · see citing works
Multiple roles for actin in secretory and endocytic pathways
Chakrabarti, R., Lee, M., & Higgs, H. N. (2021) · Current Biology · doi:10.1016/j.cub.2021.03.038 · Cited by 87 · 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 88 · see citing works
Prabhakara, C., Godbole, R. K., Sil, P., Jahnavi, S., Gulzar, S.-E.-J., van Zanten, T. S., Sheth, D., Subhash, N., Chandra, A., Shivaraj, A., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009706 · Cited by 81 · see citing works
Self-citationThe Biology of Endosomal Escape: Strategies for Enhanced Delivery of Therapeutics
Chahal, G., Helbig, K. J., Parton, R. G., & Monson, E. A. (2026) · ACS Nano · doi:10.1021/acsnano.5c18112 · Cited by 81 · see citing works
Divecha, Y. A., Rampes, S., Tromp, S., Boyanova, S., Fleckney, A. L., Fidanboylu, M., & Thomas, S. A. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100052 · Cited by 79 · see citing works
The role of lipid species in membranes and cancer-related changes
Skotland, T., Kavaliauskiene, S., & Sandvig, K. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09872-z · Cited by 69 · see citing works
Cai, W.-Q., Liang, W., Li, D., Dai, W., Li, Z., Wei, X., Cheng, L., Zhang, B., & Yang, Q.-Q. (2025) · ACS Nano · doi:10.1021/acsnano.4c14373 · Cited by 71 · see citing works
Mechanical Regulation of Endocytosis: New Insights and Recent Advances
Joseph, J. G., & Liu, A. P. (2020) · Advanced Biosystems · doi:10.1002/adbi.201900278 · Cited by 67 · see citing works
Cargo-specific recruitment in clathrin- and dynamin-independent endocytosis
Moreno‐Layseca, P., Jäntti, N. Z., Godbole, R. K., Sommer, C., Jacquemet, G., Al‐Akhrass, H., Conway, J. R. W., Kronqvist, P., Kallionpää, R., Oliveira‐Ferrer, L., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00767-x · Cited by 66 · see citing works
Self-citationExploiting cancer’s drinking problem: regulation and therapeutic potential of macropinocytosis
Puccini, J., Badgley, M. A., & Bar‐Sagi, D. (2021) · Trends in cancer · doi:10.1016/j.trecan.2021.09.004 · Cited by 67 · see citing works
Cholera Toxin as a Probe for Membrane Biology
Kenworthy, A. K., Schmieder, S. S., Raghunathan, K., Tiwari, A., Wang, T., Kelly, C. V., & Lencer, W. I. (2021) · Toxins · doi:10.3390/toxins13080543 · Cited by 59 · see citing works
Balancing lysosome abundance in health and disease
Mutvei, A. P., Nagiec, M. J., & Blenis, J. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01197-7 · Cited by 61 · see citing works
Potential therapies and diagnosis based on Golgi-targeted nano drug delivery systems
Zhang, M., Xu, N., Xu, W., Ling, G., & Zhang, P. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105861 · Cited by 54 · see citing works
Wu, J., Zhao, R., Zhao, L., Xu, Q., Jin, L., & Ma, F. (2022) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2022.129963 · Cited by 49 · see citing works
Valsalakumari, R., Yadava, S. K., Szwed, M., Pandya, A. D., Mælandsmo, G. M., Torgersen, M. L., Iversen, T., Skotland, T., Sandvig, K., & Giri, J. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.120217 · Cited by 42 · see citing works
The endocytic pathway taken by cationic substances requires Rab14 but not Rab5 and Rab7
Trofimenko, E., Homma, Y., Fukuda, M., & Widmann, C. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109945 · Cited by 40 · see citing works
Glycans in autophagy, endocytosis and lysosomal functions
Reggiori, F., Gabius, H., Aureli, M., Römer, W., Sonnino, S., & Eskelinen, E. (2021) · Glycoconjugate Journal · doi:10.1007/s10719-021-10007-x · Cited by 37 · see citing works
Unconventional endocytosis and trafficking of transferrin receptor induced by iron
Gammella, E., Lomoriello, I. S., Conte, A., Freddi, S., Alberghini, A., Poli, M., Sigismund, S., Cairo, G., & Recalcati, S. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-02-0129 · Cited by 37 · see citing works
Endocytosis-like DNA uptake by cell wall-deficient bacteria
Kapteijn, R., Shitut, S., Aschmann, D., Zhang, L., de Beer, M., Daviran, D., Roverts, R., Akiva, A., van Wezel, G. V., Kros, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33054-w · Cited by 30 · see citing works
Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins
Tsai, F., Simunovic, M., Sorre, B., Bertin, A., Manzi, J., Callan-Jones, A., & Bassereau, P. M. (2021) · Soft Matter · doi:10.1039/d0sm01573c · Cited by 33 · see citing works
Membrane-actin interactions in morphogenesis: Lessons learned from Drosophila cellularization
Sokac, A. M., Biel, N., & Renzis, S. D. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.028 · Cited by 31 · see citing works
The Curie temperature: a key playmaker in self-regulated temperature hyperthermia
Niraula, G., Wu, C., Yu, X., Malik, S., Verma, D. S., Yang, R., Zhao, B., Ding, S., Zhang, W., & Sharma, S. K. (2023) · Journal of Materials Chemistry B · doi:10.1039/d3tb01437a · Cited by 31 · see citing works
Dynamin-Independent Mechanisms of Endocytosis and Receptor Trafficking
Gundu, C., Arruri, V. K., Yadav, P., Navik, U., Kumar, A., Amalkar, V. S., Vikram, A., & Gaddam, R. R. (2022) · Cells · doi:10.3390/cells11162557 · Cited by 30 · see citing works
Transcytosis in the development and morphogenesis of epithelial tissues
Serra, N. D., & Sundaram, M. V. (2021) · The EMBO Journal · doi:10.15252/embj.2020106163 · Cited by 29 · see citing works
Caveolae as Potential Hijackable Gates in Cell Communication
Dudău, M., Codrici, E., Tănase, C., Gherghiceanu, M., Enciu, A., & Hinescu, M. E. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.581732 · Cited by 28 · see citing works
Holland, S., & Roth, R. (2023) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-09-22-0189-fi · Cited by 25 · see citing works
The Kelch13 compartment contains highly divergent vesicle trafficking proteins in malaria parasites
Schmidt, S., Wichers-Misterek, J. S., Behrens, H. M., Birnbaum, J., Henshall, I. G., Dröge, J., Jonscher, E., Flemming, S., Castro-Peña, C., Mesén-Ramírez, P., et al. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011814 · Cited by 23 · see citing works
Cell-surface glycosaminoglycans regulate the cellular uptake of charged polystyrene nanoparticles
Olivieri, P. H., de Jesus, M. B., Nader, H. B., Justo, G. Z., & Sousa, A. A. (2022) · Nanoscale · doi:10.1039/d1nr07279j · Cited by 22 · see citing works
Guo, H., Zhou, C. X., Zheng, M., Zhang, J., Wu, H., He, Q., Ding, L., & Yang, B. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107084 · Cited by 21 · see citing works
Anesthesia triggers drug delivery to experimental glioma in mice by hijacking caveolar transport
Spieth, L., Berghoff, S. A., Stumpf, S. K., Winchenbach, J., Michaelis, T., Watanabe, T., Gerndt, N., Düking, T., Hofer, S., Ruhwedel, T., et al. (2021) · Neuro-Oncology Advances · doi:10.1093/noajnl/vdab140 · Cited by 21 · see citing works
Biophysics of endocytic vesicle formation: A focus on liquid–liquid phase separation
Lomoriello, I. S., Sigismund, S., & Day, K. J. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.02.002 · Cited by 22 · see citing works
LncR26319/miR-2834/ EndophilinaA xis Regulates Oogenesis of the Silkworm, Bombyx Mori
Wang, Y., Fu, Y., Cheng, H., Zhao, C., Huang, Q., Chang, M., Qiu, W., Shen, Y., & Li, D. (2022) · Insect Science · doi:10.1111/1744-7917.13082 · Cited by 22 · see citing works
The Role and Advancement of Liposomes for Oral Diseases Therapy
Rahma, M. N., Suhandi, C., Mohammed, A. S., El‐Rayyes, A., Elamin, K. M., Sulastri, E., & Wathoni, N. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s492353 · Cited by 19 · see citing works
Ether lipids influence cancer cell fate by modulating iron uptake
Mansell, R. P., Müller, S., Yang, J.-S., Innes-Gold, S. N., Das, S., Reinhardt, F., Sigmund, K., Phadnis, V. V., Wan, Z., Stark, J. R., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-68547-5 · Cited by 22 · see citing works
Zheng, B., Pan, F., Shi, M., He, C., He, B., Wang, R., Ren, G., Yang, S., & Zhang, S. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s462374 · Cited by 21 · see citing works
Wayt, J., Cartagena‐Rivera, A. X., Dutta, D., Donaldson, J. G., & Waterman, C. M. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-07-0480 · Cited by 17 · see citing works
Kesharwani, A., Schwarz, K., Dembla, E., Dembla, M., & Schmitz, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910789 · Cited by 16 · see citing works
Endocytic trafficking of GAS6–AXL complexes is associated with sustained AKT activation
Poświata, A., Kozik, K., Miączyńska, M., & Zdżalik-Bielecka, D. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04312-3 · Cited by 17 · see citing works
Endomembranes: Unsung Heroes of Mechanobiology?
Phuyal, S., & Baschieri, F. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.597721 · Cited by 15 · see citing works
Endophilin-A2 dependent tubular endocytosis promotes plasma membrane repair and parasite invasion
Corrotte, M., Cerasoli, M., Maeda, F. Y., & Andrews, N. W. (2020) · Journal of Cell Science · doi:10.1242/jcs.249524 · Cited by 16 · see citing works
Ubiquitin and its relatives as wizards of the endolysosomal system
Berlin, I., Sapmaz, A., Stévenin, V., & Neefjes, J. (2023) · Journal of Cell Science · doi:10.1242/jcs.260101 · Cited by 15 · see citing works
Kryvenko, V., & Vadász, I. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1360370 · Cited by 15 · see citing works
Zhang, Y., Zhu, J., Xu, H., Qin, Y., Yan, L., Ye, L., Zhang, X., Xie, M., & Tan, B. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.674995 · Cited by 15 · see citing works
Signaling Pathways that Regulate Macropinocytosis in Mammalian Cells
Palm, W. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-94004-1_8 · Cited by 16 · see citing works
Hook, J. L., & Bhattacharya, J. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1328453 · Cited by 14 · see citing works
Chu, Y., Chen, M. J., Yeh, C., & Lai, M.-W. (2024) · Journal of Biomedical Science · doi:10.1186/s12929-024-01063-0 · Cited by 14 · see citing works
The roles of dynein and myosin VI motor proteins in endocytosis
Mayya, C., Hema Naveena, A., Sinha, P., Wunder, C., Johannes, L., & Bhatia, D. D. (2022) · Journal of Cell Science · doi:10.1242/jcs.259387 · Cited by 15 · see citing works
Sposini, S., Rosendale, M., Claverie, L., Van, T. N. N., Jullié, D., & Perrais, D. (2020) · Nature Protocols · doi:10.1038/s41596-020-0371-z · Cited by 14 · see citing works
N‐BAR and F‐BAR proteins—endophilin‐A3 and PSTPIP1—control clathrin‐independent endocytosis of L1CAM
Lemaigre, C., Ceuppens, A., Valades‐Cruz, C. A., Ledoux, B., Vanbeneden, B., Hassan, M., Zetterberg, F. R., Nilsson, U. J., Johannes, L., Wunder, C., et al. (2023) · Traffic · doi:10.1111/tra.12883 · Cited by 12 · see citing works
Li, S., Wang, D., He, J., Liao, C., Zuo, Z., Li, S., & Niu, X. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.70002 · Cited by 12 · see citing works
Hemifusomes and interacting proteolipid nanodroplets mediate multi-vesicular body formation
Tavakoli, A., Hu, S., Ebrahim, S., & Kachar, B. (2025) · Nature Communications · doi:10.1038/s41467-025-59887-9 · Cited by 12 · see citing works
Efficacy of Chitosan-N-Arginine Chitosomes in mRNA Delivery and Cell Viability Enhancement
Garcia, B. B. M., Douka, S., Mertins, O., Mastrobattista, E., & Han, S. W. (2024) · ACS Applied Bio Materials · doi:10.1021/acsabm.4c00983 · Cited by 11 · see citing works
Giangreco, G., Malabarba, M. G., & Sigismund, S. (2020) · Biology of the Cell · doi:10.1111/boc.202000129 · Cited by 11 · see citing works
Recent advances in the intracellular delivery of macromolecule therapeutics
Chen, S., Xu, X., Li, X., Yi, N.-B., Li, S., Xiang, X.-C., Cheng, D., & Sun, T. (2022) · Biomaterials Science · doi:10.1039/d2bm01348g · Cited by 10 · see citing works
Actin-membrane linkers: Insights from synthetic reconstituted systems
Tsai, F., Guérin, G., Pernier, J., & Bassereau, P. M. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151402 · Cited by 9 · see citing works
Mandal, T., Biswas, A., Ghosh, T., Manikandan, S. K., Kundu, A., Banerjee, A., Mitra, D., & Sinha, B. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05072-4 · Cited by 8 · see citing works
Putar, D., Čizmar, A., Chao, X., Šimić, M., Šoštar, M., Ćutić, T., Mijanović, L., Smolko, A., Tu, H., Cosson, P., et al. (2024) · Open Biology · doi:10.1098/rsob.230372 · Cited by 8 · see citing works
Li, T., Xu, B., Li, W., Cheng, X., TanTai, W., Zheng, H., Zhao, L., Li, N., & Han, C. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107096 · Cited by 8 · see citing works
Endo, A., Komada, M., & Yoshida, Y. (2024) · Bioessays · doi:10.1002/bies.202400127 · Cited by 4 · see citing works
Hema Naveena, A., & Bhatia, D. D. (2023) · ChemBioChem · doi:10.1002/cbic.202300506 · Cited by 7 · see citing works
Evaluating Cell Membrane Localization and Intracellular Transport of Proteins by Biotinylation
Reyes-Alvarez, E., Walker, T. J., & Mulligan, L. M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2376-3_15 · Cited by 7 · see citing works
Aptamers and endocytosis: The path into tumor cells
Dzarieva, F., Pavlova, S., Pavlova, G. V., & Fab, L. V. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.152960 · Cited by 6 · see citing works
Vasti, C., ́Alessandro, L. D., Bedoya, D. A., Valenti, L. E., & Giacomelli, C. E. (2025) · Hybrid Advances · doi:10.1016/j.hybadv.2025.100586 · Cited by 6 · see citing works
Li, T., Meng, H., Huang, X., Qin, Y., Sheng, S., Jiang, Y., & Ren, F. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5c03687 · Cited by 6 · see citing works
CYRI proteins: controllers of actin dynamics in the cellular ‘eat vs walk’ decision
Machesky, L. M. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221354 · Cited by 6 · see citing works
Dynein functions in galectin-3 mediated processes of clathrin-independent endocytosis
Mayya, C., Hema Naveena, A., Sinha, P., & Bhatia, D. D. (2024) · Journal of Biosciences · doi:10.1007/s12038-024-00432-z · Cited by 5 · see citing works
Dynamin independent endocytosis is an alternative cell entry mechanism for multiple animal viruses
Ojha, R., Jiang, A., Mäntylä, E., Quirin, T., Modhiran, N., Witte, R., Gaudin, A., Zanetti, L. D., Gormal, R. S., Vihinen‐Ranta, M., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012690 · Cited by 5 · see citing works
Roles of myosin 1e and the actin cytoskeleton in kidney functions and familial kidney disease
Liu, P., Sayeeda, K., Zhuang, C., & Krendel, M. (2024) · Cytoskeleton · doi:10.1002/cm.21861 · Cited by 5 · see citing works
STED Imaging of Vesicular Endocytosis in the Synapse
Hu, S., Xie, Z., Wang, B., Chen, Y., Jing, Z., Hao, Y., Yao, J., Wu, X., Huo, J., Wei, A., et al. (2024) · Neuroscience Bulletin · doi:10.1007/s12264-024-01254-7 · Cited by 5 · see citing works
Fei, J., Zheng, Y., LaLonde, C., Tao, Y., & Zhou, R. (2026) · Science Advances · doi:10.1126/sciadv.aeb0803 · Cited by 8 · see citing works
Subasic, C. N., Butcher, N. J., Simpson, F., Minchin, R. F., & Kaminskas, L. M. (2023) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c00102 · Cited by 4 · see citing works
From molecular mechanisms of glycosphingolipid function to bio-therapeutic applications
Saha, A., & Johannes, L. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06186-1 · Cited by 3 · see citing works
Guo, L., Sun, L., & Li, C. (2025) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2025.110387 · Cited by 3 · see citing works
Schmidt, S., Wichers-Misterek, J. S., Behrens, H. M., Birnbaum, J., Henshall, I. G., Dröge, J., Jonscher, E., Flemming, S., Castro-Peña, C., Mesén-Ramírez, P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.15.520209 · Cited by 3 · see citing works
Alfandari, D., Rosenhek‐Goldian, I., Kozela, E., Nevo, R., Senprún, M. B., Moisieiev, A. I., Sogauker, N., Azuri, I., Gelman, S., Kiper, E., et al. (2025) · ACS Nano · doi:10.1021/acsnano.4c07503 · Cited by 2 · see citing works
IFITM2 Modulates Endocytosis Maintaining Neural Stem Cells in Developing Neocortex
Lv, Y., Zou, W., Li, L., Zhang, S., Liang, J., Pu, J., & Jiao, J. (2025) · Advanced Science · doi:10.1002/advs.202501593 · Cited by 2 · see citing works
Sharma, P., Tanwar, M., Choudhary, E., Sundaram, N. M., Ojha, D., Mishra, L., Nain, M., Rode, A. B., Prasad, V. M., Vrati, S., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013790 · Cited by 2 · see citing works
Moraes-Lacerda, T., Garcia-Fóssa, F., & de Jesus, M. B. (2024) · Nanotechnology · doi:10.1088/1361-6528/ad4556 · Cited by 2 · see citing works
Kopach, O., Sindeeva, O. A., Zheng, K., McGowan, E., Sukhorukov, G. B., & Rusakov, D. A. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.101493 · Cited by 2 · see citing works
Galectin-3 Mediated Endocytosis of the Orphan G-Protein-Coupled Receptor GPRC5A
Boucheham, A., Franco, J. M., Bär, S., MacDonald, E., Zuttion, S., Blagec, L., Rinaldi, B., Chicher, J., Kühn, L., Hammann, P., et al. (2025) · Cells · doi:10.3390/cells14191571 · Cited by 2 · see citing works
Advances in vesicle trafficking of membrane proteins and their regulatory mechanisms
Xu, C., Qian, H., Luo, P., Yu, M., Xing, J., Zhang, L. N., Zhang, X., Cui, Y., & Lin, J. (2022) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/tb-2022-0968 · Cited by 2 · see citing works
Caveolin-1-dependent regulation of cell-matrix interphase in 3D collagen gels
Mazumdar, D., Kataria, S., Panda, G. P., Kulkarni, A., Patil, S., Dash, M., & Balasubramanian, N. (2025) · Biophysical Journal · doi:10.1016/j.bpj.2025.11.015 · Cited by 1 · see citing works
Wang, T., & Osawa, S. (2025) · Macromolecular Materials and Engineering · doi:10.1002/mame.202500319 · Cited by 1 · see citing works
Enzyme-Loaded Microcapsules as Intracellular Organelles for the Degradation of Nanoplastics by Cells
Liu, X., Chow, J., Wang, W., Dierkes, R. F., Feliu, N., Schulz, F., Streit, W. R., & Parak, W. J. (2025) · ACS Nano · doi:10.1021/acsnano.5c15213 · Cited by 1 · see citing works
Zhang, Y., Wang, C., Zhou, B., Verma, P., Hamera, S., & Zeng, L. (2026) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-02-26-0015-r · Cited by 1 · see citing works
Protein Modifications for Cellular Protein Delivery
Arafiles, J. V. V., Franke, J., Dubatouka, P., Franz, L., & Hackenberger, C. P. R. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.6c00267 · Cited by 1 · see citing works
Decoding the uptake pathway of nanoparticles in tumor cells: mechanisms, developments and challenges
Chen, Z., Zhou, L., Li, S., & Zhang, X. (2026) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2026.104054 · Cited by 1 · see citing works
Early Circulating Edema Factor in Inhalational Anthrax Infection: Does It Matter?
Tessier, E., Cheutin, L., Garnier, A., Vigne, C., Tournier, J., & Rougeaux, C. (2024) · Microorganisms · doi:10.3390/microorganisms12020308 · Cited by 1 · see citing works
- Authors
- Thottacherry, J. J., Sathe, M., Prabhakara, C., & Mayor, S.
- Affiliations
- Tata Institute of Fundamental Research (IN)
- Corresponding author
- Mayor, Satyajit
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2019-10-06
- Volume
- 35
- Issue
- 1
- Pages
- 55-84
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- PMC
- PMC6917507
- OpenAlex
- W2956919478
- Cited by
- 122
- References
- 232
- Citations by year
- 2026: 15 · 2025: 19 · 2024: 22 · 2023: 16 · 2022: 17 · 2021: 21 · 2020: 12
- FWCI
- 1.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- endocytosis, clathrin-independent endocytosis, clathrin-mediated endocytosis, cell surface, membrane tension, signal transduction regulation
- MeSH terms
- Animals, Cell Membrane, Endocytosis, Biological Evolution, Homeostasis, Humans, Signal Transduction
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