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Actin Assembly and Endocytosis: From Yeast to Mammals
Abstract
Internalization of receptors, lipids, pathogens, and other cargo at the plasma membrane involves several different pathways and requires coordinated interactions between a variety of protein and lipid molecules. The actin cytoskeleton is an integral part of the cell cortex, and there is growing evidence that F-actin plays a direct role in these endocytic events. Genetic studies in yeast have firmly established a functional connection between actin and endocytosis. Identification of several proteins that may function at the interface between actin and the endocytic machinery has provided further evidence for this association in both yeast and mammalian cells. Several of these proteins are directly involved in regulating actin assembly and could thus harness forces produced during actin polymerization to facilitate specific steps in the endocytic process. Recent microscopy studies in mammalian cells provide powerful evidence that localized recruitment and polymerization of actin occurs at endocytic sites. In this review, we focus on progress made in elucidating the functions of the actin cytoskeleton in endocytosis.
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“In yeast, active force generation by actin polymerization has been long established as the mechanism by which actin supports endocytosis85,86.”
From Membrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis (2023) · cites this paper as [86]
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Cites
Lipid rafts and signal transduction
Simons, K., & Toomre, D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 5,371
Sallusto, F., Cella, M., Danieli, C., & Lanzavecchia, A. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.2.389 · Cited by 2,501
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
Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T. L., Takenawa, T., & Kirschner, M. W. (1999) · Cell · doi:10.1016/s0092-8674(00)80732-1 · Cited by 1,350
Protein regulation by monoubiquitin
Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,227
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
Curvature of clathrin-coated pits driven by epsin
Ford, M. G. J., Mills, I. G., Peter, B. J., Vallis, Y., Praefcke, G. J. K., Evans, P. R., & McMahon, H. T. (2002) · Nature · doi:10.1038/nature01020 · Cited by 1,019
Myosins: a diverse superfamily
Sellers, J. R. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00005-7 · Cited by 850
Adams, A. E., & Pringle, J. R. (1984) · The Journal of Cell Biology · doi:10.1083/jcb.98.3.934 · Cited by 809
Salmonella interactions with host cells: type III secretion at work.
Galán, J. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.53 · Cited by 781
Research works printed but not linked: 3
- Carbone R, 1997, Cancer Res., 57, 5498
- Heuser JE, 1992, Mol. Biol. Cell, 3, 172
- Srinivasan S, 1997, Eur. J. Cell Biol., 74, 350
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Liu, J., Sun, Y., Oster, G. F., & Drubin, D. G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.009 · Cited by 70
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Michelot, A., Costanzo, M., Sarkeshik, A., Boone, C. M., Yates, J. R., & Drubin, D. G. (2010) · Current Biology · doi:10.1016/j.cub.2010.10.016 · Cited by 70
Self-citationBasquin, C., Malardé, V., Mellor, P., Anderson, D. H., Meas‐Yedid, V., Olivo‐Marín, J., Dautry‐Varsat, A., & Sauvonnet, N. (2013) · Journal of Cell Science · doi:10.1242/jcs.110932 · Cited by 69
Setiadi, H., & McEver, R. P. (2007) · Blood · doi:10.1182/blood-2007-09-113423 · Cited by 68
Cell Biology of Membrane Trafficking in Human Disease
Howell, G. J., Holloway, Z. G., Cobbold, C., Monaco, A. P., & Ponnambalam, S. (2006) · International review of cytology · doi:10.1016/s0074-7696(06)52005-4 · Cited by 68
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Mathur, J. (2005) · BioEssays · doi:10.1002/bies.20206 · Cited by 68
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Uruno, T., Remmert, K., & Hammer, J. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513186200 · Cited by 67
Lysosomal cysteine peptidases – Molecules signaling tumor cell death and survival
Pišlar, A. H., Nanut, M. P., & Kos, J. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.08.001 · Cited by 66
Sattlegger, E., Swanson, M. J., Ashcraft, E. A., Jennings, J. L., Fekete, R. A., Link, A. J., & Hinnebusch, A. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404009200 · Cited by 66
Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding
Baek, K., Liu, X., Ferrón, F., Shu, S., Korn, E. D., & Domínguez, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805852105 · Cited by 65
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Kim, K., Galletta, B. J., Schmidt, K. O., Chang, F. S., Blumer, K., & Cooper, J. A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-10-0925 · Cited by 65
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Parkar, N. S., Akpa, B. S., Nitsche, L. C., Wedgewood, L. E., Place, A. T., Sverdlov, M. S., Chaga, O. Y., & Minshall, R. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2397 · Cited by 64
Actin is required for endocytic trafficking in the malaria parasite Plasmodium falciparum
Smythe, W. A., Joiner, K. A., & Hoppe, H. C. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.01058.x · Cited by 63
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Meriin, A. B., Zhang, X., Alexandrov, I. M., Salnikova, A. B., Ter-Avanesian, M. D., Chernoff, Y. O., & Sherman, M. Y. (2007) · The FASEB Journal · doi:10.1096/fj.06-6878com · Cited by 62
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Stanasila, L., Abuin, L., Diviani, D., & Cotecchia, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511989200 · Cited by 62
Imaging and Modeling the Dynamics of Clathrin-Mediated EndocytosisPreprint
Mettlen, M., & Danuser, G. M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a017038 · Cited by 62
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Cheng, X., Chen, K., Dong, B., Yang, M., Filbrun, S. L., Myoung, Y., Huang, T.-X., Gu, Y. H., Wang, G., & Fang, N. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00713-x · Cited by 62
Feliciano, D., & Pietro, S. M. D. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-12-1022 · Cited by 60
Eyster, C. A., Duggins, Q. S., & Olson, A. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409806200 · Cited by 60
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Takeda, T., & Chang, F. (2005) · Current Biology · doi:10.1016/j.cub.2005.07.009 · Cited by 60
Nardo, A. D., Cicchetti, G., Falet, H., Hartwig, J. H., Stossel, T. P., & Kwiatkowski, D. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508228102 · Cited by 60
An unmet actin requirement explains the mitotic inhibition of clathrin-mediated endocytosis
Kaur, S., Fielding, A. B., Gassner, G., Carter, N. J., & Royle, S. (2014) · eLife · doi:10.7554/elife.00829 · Cited by 59
Rodríguez‐Fernández, J. L., & Criado‐García, O. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00528 · Cited by 58
Niiro, H., Allam, A., Stoddart, A., Brodsky, F. M., Marshall, A. J., & Clark, E. A. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.9.5601 · Cited by 58
Ono, K., & Ono, S. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-03-0179 · Cited by 58
Mechanics and regulation of cytokinesis in budding yeast
Bhavsar-Jog, Y. P., & Bi, E. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.12.010 · Cited by 57
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Lorusso, A., Covino, C., Priori, G., Bachi, A., Meldolesi, J., & Chieregatti, E. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601419 · Cited by 56
Global and Local Regulation of Clathrin-Coated Pit Dynamics Detected on Patterned Substrates
Liu, A. P., Loerke, D., Schmid, S. L., & Danuser, G. M. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.06.003 · Cited by 56
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Flower, T. R., Clark-Dixon, C., Metoyer, C. F., Yang, H., Shi, R., Zhang, Z., & Witt, S. N. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610071 · Cited by 56
Dada, L. A., Novoa, E. M., Lecuona, E., Sun, H., & Sznajder, J. I. (2007) · Journal of Cell Science · doi:10.1242/jcs.003038 · Cited by 56
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Mason, R. P., & Giorgini, F. (2011) · Prion · doi:10.4161/pri.18005 · Cited by 55
Vogler, M., Vogel, S., Krull, S., Farhat, K., Leisering, P., Lutz, S., Wuertz, C. M., Katschinski, D. M., & Zieseniß, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069128 · Cited by 56
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Knoblauch, M., & Peters, W. S. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4158-0 · Cited by 53
Koike, S., Keino‐Masu, K., Ohto, T., Sugiyama, F., Takahashi, S., & Masu, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.012716 · Cited by 52
Pan, F., Égile, C., Lipkin, T. G., & Li, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402357200 · Cited by 52
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“In yeast, active force generation by actin polymerization has been long established as the mechanism by which actin supports endocytosis 85,86 .”
Douglas, L. M., Martin, S. W., & Konopka, J. B. (2009) · Infection and Immunity · doi:10.1128/iai.00683-09 · Cited by 51
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Wu, K., Jerdeva, G. V., da Costa, S. R., Sou, E., Schechter, J., & Hamm‐Alvarez, S. F. (2006) · Experimental Eye Research · doi:10.1016/j.exer.2005.11.009 · Cited by 50
Sevrioukov, E. A., Moghrabi, N. N., Kuhn, M., & Krämer, H. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-11-1013 · Cited by 50
Strádalová, V., Blažíková, M., Großmann, G., Opekarová, M., Tanner, W., & Malínský, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035132 · Cited by 49
Bradley, S. V., Hyun, T. S., Oravecz-Wilson, K. I., Li, L., Waldorff, E. I., Ermilov, A. N., Goldstein, S. A., Zhang, C. X., Drubin, D. G., Varela, K., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm076 · Cited by 49
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Gaidarov, I., Zhao, Y., & Keen, J. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507731200 · Cited by 48
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Xia, W., Liang, Y., Chi, Y., Pan, L., Zhao, J., Liu, S., & Wang, X. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006866 · Cited by 48
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Aniento, F., & Robinson, D. G. (2005) · PROTOPLASMA · doi:10.1007/s00709-005-0101-y · Cited by 48
Chang, F. S., Han, G., Carman, G. M., & Blumer, K. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200501086 · Cited by 48
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Xiang, X., Qiu, R., Yao, X., Arst, H. N., Peñalva, M. A., & Zhang, J. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1926-y · Cited by 48
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Wagh, D. A., Terry-Lorenzo, R. T., Waites, C. L., Leal‐Ortiz, S., Maas, C., Reimer, R. J., & Garner, C. C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120093 · Cited by 47
Toshima, J., Toshima, J. Y., Duncan, M. C., Cope, M. J. T. V., Sun, Y., Martin, A. C., Anderson, S., Yates, J. R., Mizuno, K., & Drubin, D. G. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0788 · Cited by 47
Self-citationCabrera, I. E., Pacentine, I. V., Lim, A., Guerrero, N., Kryštofová, S., Li, L., Michkov, A. V., Servin, J. A., Ahrendt, S. R., Carrillo, A. J., et al. (2015) · G3 Genes Genomes Genetics · doi:10.1534/g3.115.020974 · Cited by 47
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Juanes, M. A., & Piatti, S. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2220-3 · Cited by 47
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Rizzelli, F., Malabarba, M. G., Sigismund, S., & Mapelli, M. (2020) · Open Biology · doi:10.1098/rsob.190314 · Cited by 47
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Brett, T. J., & Traub, L. M. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.014 · Cited by 47
Boettner, D. R., Friesen, H., Andrews, B., & Lemmon, S. K. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-07-0628 · Cited by 46
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Kishimoto, T., Yamamoto, T. G., & Tanaka, K. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-05-0452 · Cited by 46
Wen, K., & Rubenstein, P. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502024200 · Cited by 45
Yu, H.-Y. E., & Bement, W. M. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-11-0993 · Cited by 45
Badizadegan, K., Wheeler, H. E., Fujinaga, Y., & Lencer, W. I. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00189.2004 · Cited by 45
Toshima, J. Y., Nakanishi, J.-I., Mizuno, K., Toshima, J., & Drubin, D. G. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0541 · Cited by 44
Self-citationGuo, F., Ma, N., Horibe, Y., Kawanishi, S., Murata, M., & Hiraku, Y. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.02.010 · Cited by 43
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Stollar, E. J., Garcı́a, B., Chong, P. A., Rath, A., Lin, H., Forman-Kay, J. D., & Davidson, A. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028431 · Cited by 43
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Ćurak, J., Rohde, J. R., & Štagljar, I. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.11.004 · Cited by 43
Bourne, J. N., Morgan, J. R., & Pieribone, V. A. (2006) · The Journal of Comparative Neurology · doi:10.1002/cne.21006 · Cited by 43
Klima, A., & Foissner, I. (2008) · Plant and Cell Physiology · doi:10.1093/pcp/pcn122 · Cited by 43
Kapetanovich, L., Baughman, C. B., & Lee, T. H. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-09-0785 · Cited by 43
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Sakane, H., Yamamoto, T. G., & Tanaka, K. (2006) · Cell Structure and Function · doi:10.1247/csf.06021 · Cited by 42
Clark, M. G., Teply, J., Haarer, B. K., Viggiano, S. C., Sept, D., & Amberg, D. C. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-10-0956 · Cited by 42
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Nagasato, C., Inoue, A., Mizuno, M., Kanazawa, K., Ojima, T., Okuda, K., & Motomura, T. (2010) · Planta · doi:10.1007/s00425-010-1188-8 · Cited by 40
Sun, Y., Schöneberg, J., Chen, X., Jiang, T., Kaplan, C., Xu, K., Pollard, T. D., & Drubin, D. G. (2019) · eLife · doi:10.7554/elife.50749 · Cited by 40
Self-citationBarker, S. L., Lee, L., Pierce, B. D., Maldonado‐Báez, L., Drubin, D. G., & Wendland, B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-05-0436 · Cited by 40
Self-citationMcKane, M., Wen, K., Meyer, A., & Rubenstein, P. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602251200 · Cited by 40
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Chierico, L., Joseph, A. S., Lewis, A. L., & Battaglia, G. (2014) · Scientific Reports · doi:10.1038/srep06056 · Cited by 39
Brady, R. J., Damer, C. K., Heuser, J. E., & O’Halloran, T. J. (2010) · Journal of Cell Science · doi:10.1242/jcs.066852 · Cited by 39
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Ojala, K. S., Reedich, E. J., DiDonato, C. J., & Meriney, S. D. (2021) · Brain Sciences · doi:10.3390/brainsci11020194 · Cited by 37
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Kabayama, H., Takeuchi, M., Taniguchi, M., Tokushige, N., Kozaki, S., Mizutani, A., Nakamura, T., & Mikoshiba, K. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.2718-10.2011 · Cited by 37
Laroche, G., Rochdi, M. D., Laporte, S. A., & Parent, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414071200 · Cited by 37
Rapid production of pure recombinant actin isoforms in Pichia pastoris
Hatano, T., Alioto, S. L., Roscioli, E., Palani, S., Clarke, S. T., Kamnev, A., Hernandez-Fernaud, J. R., Sivashanmugam, L., Chapa‐y‐Lazo, B., Jones, A. M. E., et al. (2018) · Journal of Cell Science · doi:10.1242/jcs.213827 · Cited by 36
Haynes, J., Garcı́a, B., Stollar, E. J., Rath, A., Andrews, B., & Davidson, A. R. (2007) · Genetics · doi:10.1534/genetics.106.070300 · Cited by 36
Quintero‐Monzon, O., Rodal, A. A., Strokopytov, B. V., Almo, S. C., & Goode, B. L. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0059 · Cited by 36
Buser, C., & Drubin, D. G. (2013) · Microscopy and Microanalysis · doi:10.1017/s1431927612014304 · Cited by 35
Self-citationMolecular mechanisms for regulation of AMPAR trafficking by PICK1
Hanley, J. G. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340931 · Cited by 35
Intersectin adaptor proteins are associated with actin-regulating protein WIP in invadopodia
Gryaznova, T. A., Kropyvko, S. V., Burdyniuk, M., Gubar, O. S., Kryklyva, V., Tsyba, L., & Rynditch, A. V. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.03.006 · Cited by 34
Tuba, A GEF for CDC42, Links Dynamin to Actin Regulatory Proteins
Cestra, G., Kwiatkowski, A. V., Salazar, M. A. G., Gertler, F. B., & Camilli, P. V. D. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)04047-4 · Cited by 34
Volovyk, Z. M., Wolf, M. J., Prasad, S. V. N., & Rockman, H. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511435200 · Cited by 34
Yoshida, A., Wei, D., Nomura, W., Izawa, S., & Inoue, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322222 · Cited by 34
Trans-endocytosis of CD47 and SHPS-1 and its role in regulation of the CD47–SHPS-1 system
Kusakari, S., Ohnishi, H., Jin, F.-J., Kaneko, Y., Murata, T., Murata, Y., Okazawa, H., & Matozaki, T. (2008) · Journal of Cell Science · doi:10.1242/jcs.025015 · Cited by 34
Gao, L., & Bretscher, A. P. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-05-0520 · Cited by 34
Metadata
- Authors
- Engqvist-Goldstein, Å. E. Y., & Drubin, D. G.
- Affiliations
- University of California, Berkeley (US)
- ORCID
- Drubin, David G.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2003-11
- Volume
- 19
- Issue
- 1
- Pages
- 287-332
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2144535282
- Cited by
- 572
- References
- 228
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 7 · 2023: 5 · 2022: 10 · 2021: 15 · 2020: 11 · 2019: 7 · 2018: 18 · 2017: 15 · 2016: 11 · 2015: 18 · 2014: 24 · 2013: 22 · 2012: 21
- FWCI
- 4.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- actin cytoskeleton, endocytosis, F-actin polymerization, actin assembly, plasma membrane internalization, cell cortex, yeast genetics, mammalian cells, receptor internalization, pathogen internalization
- MeSH terms
- Actins, Animals, Clathrin, Endocytosis, Humans, Actin Cytoskeleton, Yeasts, Caveolae, Cell Membrane Structures, Saccharomyces cerevisiae Proteins, Dynamins, Actin-Related Protein 2
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