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Volumn 19, Issue , 2003, Pages 287-332

Actin Assembly and Endocytosis: From Yeast to Mammals

Author keywords

Arp2 3 complex; Caveolae; Clathrin; Dynamin; Macropinocytosis

Indexed keywords

ACTIN; CLATHRIN; DYNAMIN; F ACTIN; LIPID;

EID: 0041721457     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.19.111401.093127     Document Type: Conference Paper
Times cited : (502)

References (227)
  • 1
    • 0021355377 scopus 로고
    • Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae
    • Adams AE, Pringle JR. 1984. Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J. Cell Biol. 98:934-45
    • (1984) J. Cell Biol. , vol.98 , pp. 934-945
    • Adams, A.E.1    Pringle, J.R.2
  • 2
    • 0037518120 scopus 로고    scopus 로고
    • The yeast epsin Ent1 is recruited to membranes through multiple independent interactions
    • Aguilar RC, Watson HA, Wendland B. 2003. The yeast epsin Ent1 is recruited to membranes through multiple independent interactions. J. Biol. Chem. 278:10737-43
    • (2003) J. Biol. Chem. , vol.278 , pp. 10737-10743
    • Aguilar, R.C.1    Watson, H.A.2    Wendland, B.3
  • 3
    • 0035009245 scopus 로고    scopus 로고
    • Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton
    • Apodaca G. 2001. Endocytic traffic in polarized epithelial cells: role of the actin and microtubule cytoskeleton. Traffic 2:149-59
    • (2001) Traffic , vol.2 , pp. 149-159
    • Apodaca, G.1
  • 4
    • 0034649660 scopus 로고    scopus 로고
    • Endocytosis and the development of cell polarity in yeast require a dynamic F-actin cytoskeleton
    • Ayscough KR. 2000. Endocytosis and the development of cell polarity in yeast require a dynamic F-actin cytoskeleton. Curr. Biol. 10:1587-90
    • (2000) Curr. Biol. , vol.10 , pp. 1587-1590
    • Ayscough, K.R.1
  • 5
    • 0032934806 scopus 로고    scopus 로고
    • Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology
    • Ayscough KR, Eby JJ, Lila T, Dewar H, Kozminski KG, Drubin DG. 1999. Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology. Mol. Biol. Cell 10:1061-75
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1061-1075
    • Ayscough, K.R.1    Eby, J.J.2    Lila, T.3    Dewar, H.4    Kozminski, K.G.5    Drubin, D.G.6
  • 6
    • 0030978526 scopus 로고    scopus 로고
    • High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A
    • Ayscough KR, Stryker J, Pokala N, Sanders M, Crews P, Drubin DG. 1997. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. J. Cell Biol. 137:399-416
    • (1997) J. Cell Biol. , vol.137 , pp. 399-416
    • Ayscough, K.R.1    Stryker, J.2    Pokala, N.3    Sanders, M.4    Crews, P.5    Drubin, D.G.6
  • 7
    • 0035006256 scopus 로고    scopus 로고
    • Clathrin function in yeast endocytosis
    • Baggett JJ, Wendland B. 2001. Clathrin function in yeast endocytosis. Traffic 2:297-302
    • (2001) Traffic , vol.2 , pp. 297-302
    • Baggett, J.J.1    Wendland, B.2
  • 8
    • 0027219273 scopus 로고
    • Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns
    • Bauer F, Urdaci M, Aigle M, Crouzet M. 1993. Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns. Mol. Cell. Biol. 13:5070-84
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5070-5084
    • Bauer, F.1    Urdaci, M.2    Aigle, M.3    Crouzet, M.4
  • 9
    • 0032494082 scopus 로고    scopus 로고
    • The yeast V159N actin mutant reveals roles for actin dynamics in vivo
    • Belmont LD, Drubin DG. 1998. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 142:1289-99
    • (1998) J. Cell Biol. , vol.142 , pp. 1289-1299
    • Belmont, L.D.1    Drubin, D.G.2
  • 10
  • 12
    • 0035157924 scopus 로고    scopus 로고
    • Clathrin hub expression dissociates the actin-binding protein Hip1R from coated pits and disrupts their alignment with the actin cytoskeleton
    • Bennett EM, Chen CY, Engqvist-Goldstein ÅE, Drubin DG, Brodsky FM. 2001. Clathrin hub expression dissociates the actin-binding protein Hip1R from coated pits and disrupts their alignment with the actin cytoskeleton. Traffic 2:851-58
    • (2001) Traffic , vol.2 , pp. 851-858
    • Bennett, E.M.1    Chen, C.Y.2    Engqvist-Goldstein, Å.E.3    Drubin, D.G.4    Brodsky, F.M.5
  • 13
    • 0033527066 scopus 로고    scopus 로고
    • An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation
    • Bowden ET, Barth M, Thomas D, Glazer RI, Mueller SC. 1999. An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation. Oncogene 18:4440-49
    • (1999) Oncogene , vol.18 , pp. 4440-4449
    • Bowden, E.T.1    Barth, M.2    Thomas, D.3    Glazer, R.I.4    Mueller, S.C.5
  • 14
    • 0342748583 scopus 로고    scopus 로고
    • Sequential steps in clathrin-mediated synaptic vesicle endocytosis
    • Brodin L, Low P, Shupliakov O. 2000. Sequential steps in clathrin-mediated synaptic vesicle endocytosis. Curr. Opin. Neurobiol. 10:312-20
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 312-320
    • Brodin, L.1    Low, P.2    Shupliakov, O.3
  • 16
    • 0035898659 scopus 로고    scopus 로고
    • Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis
    • Buss F, Arden SD, Lindsay M, Luzio JP, Kendrick-Jones J. 2001. Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis. EMBO J. 20:3676-84
    • (2001) EMBO J. , vol.20 , pp. 3676-3684
    • Buss, F.1    Arden, S.D.2    Lindsay, M.3    Luzio, J.P.4    Kendrick-Jones, J.5
  • 17
    • 0036901155 scopus 로고    scopus 로고
    • Myosin VI, an actin motor for membrane traffic and cell migration
    • Buss F, Luzio JP, Kendrick-Jones J. 2002. Myosin VI, an actin motor for membrane traffic and cell migration. Traffic 3:851-58
    • (2002) Traffic , vol.3 , pp. 851-858
    • Buss, F.1    Luzio, J.P.2    Kendrick-Jones, J.3
  • 18
    • 0037371802 scopus 로고    scopus 로고
    • Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis
    • Cao H, Orth JD, Chen J, Weller SG, Heuser JE, McNiven MA. 2003. Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis. Mol. Cell Biol. 23:2162-70
    • (2003) Mol. Cell Biol. , vol.23 , pp. 2162-2170
    • Cao, H.1    Orth, J.D.2    Chen, J.3    Weller, S.G.4    Heuser, J.E.5    McNiven, M.A.6
  • 19
    • 0031452290 scopus 로고    scopus 로고
    • eps15 and eps15R are essential components of the endocytic pathway
    • Carbone R, Fre S, Iannolo G, Belleudi F, Mancini P, et al. 1997. eps15 and eps15R are essential components of the endocytic pathway. Cancer Res. 57:5498-504
    • (1997) Cancer Res. , vol.57 , pp. 5498-5504
    • Carbone, R.1    Fre, S.2    Iannolo, G.3    Belleudi, F.4    Mancini, P.5
  • 20
    • 0034998063 scopus 로고    scopus 로고
    • Phagocytosis and macropinocytosis in Dictyostelium: Phosphoinositide- based processes, biochemically distinct
    • Cardelli J. 2001. Phagocytosis and macropinocytosis in Dictyostelium: phosphoinositide-based processes, biochemically distinct. Traffic 2:311-20
    • (2001) Traffic , vol.2 , pp. 311-320
    • Cardelli, J.1
  • 21
    • 0032552056 scopus 로고    scopus 로고
    • Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
    • Chen H, Fre S, Slepnev VI, Capua MR, Takei K, et al. 1998. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 394:793-97
    • (1998) Nature , vol.394 , pp. 793-797
    • Chen, H.1    Fre, S.2    Slepnev, V.I.3    Capua, M.R.4    Takei, K.5
  • 22
    • 0033769138 scopus 로고    scopus 로고
    • HIP12 is a non-proapoptotic member of a gene family including HIP1, an interacting protein with huntingtin
    • Chopra VS, Metzler M, Rasper DM, Engqvist-Goldstein AE, Singaraja R, et al. 2000. HIP12 is a non-proapoptotic member of a gene family including HIP1, an interacting protein with huntingtin. Mamm. Genome 11:1006-15
    • (2000) Mamm. Genome , vol.11 , pp. 1006-1015
    • Chopra, V.S.1    Metzler, M.2    Rasper, D.M.3    Engqvist-Goldstein, A.E.4    Singaraja, R.5
  • 23
    • 0033594087 scopus 로고    scopus 로고
    • Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast
    • Cope MJ, Yang S, Shang C, Drubin DG. 1999. Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast. J. Cell Biol. 144:1203-18
    • (1999) J. Cell Biol. , vol.144 , pp. 1203-1218
    • Cope, M.J.1    Yang, S.2    Shang, C.3    Drubin, D.G.4
  • 24
    • 0035074215 scopus 로고    scopus 로고
    • Phosphoinositides in membrane traffic at the synapse
    • Cremona O, De Camilli P. 2001. Phosphoinositides in membrane traffic at the synapse. J. Cell Sci. 114:1041-52
    • (2001) J. Cell Sci. , vol.114 , pp. 1041-1052
    • Cremona, O.1    De Camilli, P.2
  • 25
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke H, Baba T, Warnock DE, Schmid SL. 1994. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127:915-34
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 26
    • 0037106464 scopus 로고    scopus 로고
    • Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiae
    • Desrivieres S, Cooke FT, Morales-Johansson H, Parker PJ, Hall MN. 2002. Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiae. Biochem. J. 366:945-51
    • (2002) Biochem. J. , vol.366 , pp. 945-951
    • Desrivieres, S.1    Cooke, F.T.2    Morales-Johansson, H.3    Parker, P.J.4    Hall, M.N.5
  • 29
    • 0027488669 scopus 로고
    • A proline-rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae
    • Donnelly SF, Pocklington MJ, Pallotta D, Orr E. 1993. A proline-rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 10:585-96
    • (1993) Mol. Microbiol. , vol.10 , pp. 585-596
    • Donnelly, S.F.1    Pocklington, M.J.2    Pallotta, D.3    Orr, E.4
  • 30
    • 0029966290 scopus 로고    scopus 로고
    • Movement of yeast cortical actin cytoskeleton visualized in vivo
    • Doyle T, Botstein D. 1996. Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc. Natl. Acad. Sci. USA 93:3886-91
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3886-3891
    • Doyle, T.1    Botstein, D.2
  • 31
    • 0032407404 scopus 로고    scopus 로고
    • Intracellular pathogens and the actin cytoskeleton
    • Dramsi S, Cossart P. 1998. Intracellular pathogens and the actin cytoskeleton. Annu. Rev. Cell Dev. Biol. 14:137-66
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 137-166
    • Dramsi, S.1    Cossart, P.2
  • 34
    • 0034663146 scopus 로고    scopus 로고
    • F-actin is concentrated in nonrelease domains at frog neuromuscular junctions
    • Dunaevsky A, Connor EA. 2000. F-actin is concentrated in nonrelease domains at frog neuromuscular junctions. J. Neurosci. 20:6007-12
    • (2000) J. Neurosci. , vol.20 , pp. 6007-6012
    • Dunaevsky, A.1    Connor, E.A.2
  • 36
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn R, Hicke L. 2001. Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 276:25974-81
    • (2001) J. Biol. Chem. , vol.276 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 37
    • 0033611051 scopus 로고    scopus 로고
    • An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles
    • Engqvist-Goldstein ÅE, Kessels MM, Chopra VS, Hayden MR, Drubin DG. 1999. An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J. Cell Biol. 147:1503-18
    • (1999) J. Cell Biol. , vol.147 , pp. 1503-1518
    • Engqvist-Goldstein, Å.E.1    Kessels, M.M.2    Chopra, V.S.3    Hayden, M.R.4    Drubin, D.G.5
  • 38
    • 0035904239 scopus 로고    scopus 로고
    • The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro
    • Engqvist-Goldstein ÅE, Warren RA, Kessels MM, Keen JH, Heuser J, Drubin DG. 2001. The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro. J. Cell Biol. 154:1209-23
    • (2001) J. Cell Biol. , vol.154 , pp. 1209-1223
    • Engqvist-Goldstein, Å.E.1    Warren, R.A.2    Kessels, M.M.3    Keen, J.H.4    Heuser, J.5    Drubin, D.G.6
  • 39
    • 0034707598 scopus 로고    scopus 로고
    • A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex
    • Evangelista M, Klebl BM, Tong AH, Webb BA, Leeuw T, et al. 2000. A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex. J. Cell Biol. 148:353-62
    • (2000) J. Cell Biol. , vol.148 , pp. 353-362
    • Evangelista, M.1    Klebl, B.M.2    Tong, A.H.3    Webb, B.A.4    Leeuw, T.5
  • 40
    • 0033934481 scopus 로고    scopus 로고
    • Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane
    • Feng Y, Davis NG. 2000. Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane. Mol. Cell. Biol. 20:5350-59
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5350-5359
    • Feng, Y.1    Davis, N.G.2
  • 43
    • 0028920045 scopus 로고
    • An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein
    • Freeman NL, Chen Z, Horenstein J, Weber A, Field J. 1995. An actin monomer binding activity localizes to the carboxyl-terminal half of the Saccharomyces cerevisiae cyclase-associated protein. J. Biol. Chem. 270:5680-85
    • (1995) J. Biol. Chem. , vol.270 , pp. 5680-5685
    • Freeman, N.L.1    Chen, Z.2    Horenstein, J.3    Weber, A.4    Field, J.5
  • 44
    • 0033613455 scopus 로고    scopus 로고
    • Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling
    • Frischknecht F, Moreau V, Rottger S, Gonfloni S, Reckmann I, et al. 1999. Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling. Nature 401:926-29
    • (1999) Nature , vol.401 , pp. 926-929
    • Frischknecht, F.1    Moreau, V.2    Rottger, S.3    Gonfloni, S.4    Reckmann, I.5
  • 45
    • 0034139820 scopus 로고    scopus 로고
    • Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells
    • Fujimoto LM, Roth R, Heuser JE, Schmid SL. 2000. Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells. Traffic 1:161-71
    • (2000) Traffic , vol.1 , pp. 161-171
    • Fujimoto, L.M.1    Roth, R.2    Heuser, J.E.3    Schmid, S.L.4
  • 46
    • 0033678935 scopus 로고    scopus 로고
    • Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin
    • Gad H, Ringstad N, Low P, Kjaerulff O, Gustafsson J, et al. 2000. Fission and uncoating of synaptic clathrin-coated vesicles are perturbed by disruption of interactions with the SH3 domain of endophilin. Neuron 27:301-12
    • (2000) Neuron , vol.27 , pp. 301-312
    • Gad, H.1    Ringstad, N.2    Low, P.3    Kjaerulff, O.4    Gustafsson, J.5
  • 47
    • 0033598129 scopus 로고    scopus 로고
    • Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits
    • Gaidarov I, Keen JH. 1999. Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits. J. Cell Biol. 146:755-64
    • (1999) J. Cell Biol. , vol.146 , pp. 755-764
    • Gaidarov, I.1    Keen, J.H.2
  • 49
    • 0035188434 scopus 로고    scopus 로고
    • Salmonella interactions with host cells: Type III secretion at work
    • Galán JE. 2001. Salmonella interactions with host cells: type III secretion at work. Annu. Rev. Cell Dev. Biol. 17:53-86
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 53-86
    • Galán, J.E.1
  • 50
    • 0034604337 scopus 로고    scopus 로고
    • Developmental control of endocytosis in dendritic cells by Cdc42
    • Garrett WS, Chen LM, Kroschewski R, Ebersold M, Turley S, et al. 2000. Developmental control of endocytosis in dendritic cells by Cdc42. Cell 102:325-34
    • (2000) Cell , vol.102 , pp. 325-334
    • Garrett, W.S.1    Chen, L.M.2    Kroschewski, R.3    Ebersold, M.4    Turley, S.5
  • 51
    • 0034663930 scopus 로고    scopus 로고
    • An intact SH3 domain is required for myosin I-induced actin polymerization
    • Geli MI, Lombardi R, Schmelzl B, Riezman H. 2000. An intact SH3 domain is required for myosin I-induced actin polymerization. EMBO J. 19:4281-91
    • (2000) EMBO J. , vol.19 , pp. 4281-4291
    • Geli, M.I.1    Lombardi, R.2    Schmelzl, B.3    Riezman, H.4
  • 52
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli MI, Riezman H. 1996. Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272:533-35
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 53
    • 0036173770 scopus 로고    scopus 로고
    • Recruitment and activation of caspase-8 by the Huntingtin-interacting proteins Hip-1 and a novel partner Hippi
    • Gervais FG, Singaraja R, Xanthoudakis S, Gutekunst CA, Leavitt BR, et al. 2002. Recruitment and activation of caspase-8 by the Huntingtin-interacting proteins Hip-1 and a novel partner Hippi. Nat. Cell Biol. 4:95-105
    • (2002) Nat. Cell Biol. , vol.4 , pp. 95-105
    • Gervais, F.G.1    Singaraja, R.2    Xanthoudakis, S.3    Gutekunst, C.A.4    Leavitt, B.R.5
  • 55
    • 0035199446 scopus 로고    scopus 로고
    • Modular complexes that regulate actin assembly in budding yeast
    • Goode BL, Rodal AA. 2001. Modular complexes that regulate actin assembly in budding yeast. Curr. Opin. Microbiol. 4:703-12
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 703-712
    • Goode, B.L.1    Rodal, A.A.2
  • 56
    • 0035972165 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the actin filament binding protein Abp1p
    • Goode BL, Rodal AA, Barnes G, Drubin DG. 2001. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J. Cell Biol. 153:627-34
    • (2001) J. Cell Biol. , vol.153 , pp. 627-634
    • Goode, B.L.1    Rodal, A.A.2    Barnes, G.3    Drubin, D.G.4
  • 57
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman OB Jr, Krupnick JG, Gurevich W, Benovic JL, Keen JH. 1997. Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J. Biol. Chem. 272:15017-22
    • (1997) J. Biol. Chem. , vol.272 , pp. 15017-15022
    • Goodman Jr., O.B.1    Krupnick, J.G.2    Gurevich, W.3    Benovic, J.L.4    Keen, J.H.5
  • 58
    • 0029984773 scopus 로고    scopus 로고
    • Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
    • Goodson HV, Anderson BL, Warrick HM, Pon LA, Spudich JA. 1996. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton. J. Cell Biol. 133:1277-91
    • (1996) J. Cell Biol. , vol.133 , pp. 1277-1291
    • Goodson, H.V.1    Anderson, B.L.2    Warrick, H.M.3    Pon, L.A.4    Spudich, J.A.5
  • 59
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb TA, Ivanov IE, Adesnik M, Sabatini DD. 1993. Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J Cell Biol. 120:695-710
    • (1993) J Cell Biol. , vol.120 , pp. 695-710
    • Gottlieb, T.A.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 60
    • 0032211687 scopus 로고    scopus 로고
    • Two isoforms of a human intersectin (ITSN) protein are produced by brain-specific alternative splicing in a stop codon
    • Guipponi M, Scott HS, Chen H, Schebesta A, Rossier C, Antonarakis SE. 1998. Two isoforms of a human intersectin (ITSN) protein are produced by brain-specific alternative splicing in a stop codon. Genomics 53:369-76
    • (1998) Genomics , vol.53 , pp. 369-376
    • Guipponi, M.1    Scott, H.S.2    Chen, H.3    Schebesta, A.4    Rossier, C.5    Antonarakis, S.E.6
  • 61
    • 0031046060 scopus 로고    scopus 로고
    • Fluidphase uptake by macropinocytosis in Dictyostelium
    • Hacker U, Albrecht R, Maniak M. 1997. Fluidphase uptake by macropinocytosis in Dictyostelium. J. Cell Sci. 110(Pt 2): 105-12
    • (1997) J. Cell Sci. , vol.110 , Issue.2 PART , pp. 105-112
    • Hacker, U.1    Albrecht, R.2    Maniak, M.3
  • 62
    • 0031434562 scopus 로고    scopus 로고
    • Synaptojanin 1: Localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15
    • Haffner C, Takei K, Chen H, Ringstad N, Hudson A, et al. 1997. Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. FEBS Lett. 419:175-80
    • (1997) FEBS Lett. , vol.419 , pp. 175-180
    • Haffner, C.1    Takei, K.2    Chen, H.3    Ringstad, N.4    Hudson, A.5
  • 65
    • 0036679002 scopus 로고    scopus 로고
    • Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of Sla2p in yeast
    • Henry KR, D'Hondt K, Chang J, Newpher T, Huang K, et al. 2002. Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of Sla2p in yeast. Mol. Biol. Cell 13:2607-25
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2607-2625
    • Henry, K.R.1    D'Hondt, K.2    Chang, J.3    Newpher, T.4    Huang, K.5
  • 66
    • 0000131826 scopus 로고
    • Time-lapse video microscopy of endosomal "rocketing" of La/Zn-treated cells
    • Abstr.
    • Heuser JE, Morisaki JH. 1992. Time-lapse video microscopy of endosomal "rocketing" of La/Zn-treated cells. Mol. Biol. Cell 3:172 (Abstr.)
    • (1992) Mol. Biol. Cell , vol.3 , pp. 172
    • Heuser, J.E.1    Morisaki, J.H.2
  • 67
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. 2001. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2:195-201
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 68
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke L, Riezman H. 1996. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84:277-87
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 69
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization
    • Hicke L, Zanolari B, Riezman H. 1998. Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization. J. Cell Biol. 141:349-58
    • (1998) J. Cell Biol. , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 70
    • 0036558028 scopus 로고    scopus 로고
    • Snap-shots of clathrin-mediated endocytosis
    • Higgins MK, McMahon HT. 2002. Snap-shots of clathrin-mediated endocytosis. Trends Biochem. Sci. 27:257-63
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 257-263
    • Higgins, M.K.1    McMahon, H.T.2
  • 71
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw JE. 2000. Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16:483-519
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 72
    • 0027244817 scopus 로고
    • Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae
    • Holtzman DA, Yang S, Drubin DG. 1993. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. J. Cell Biol. 122:635-44
    • (1993) J. Cell Biol. , vol.122 , pp. 635-644
    • Holtzman, D.A.1    Yang, S.2    Drubin, D.G.3
  • 74
    • 0032476012 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells
    • Huang C, Liu J, Haudenchild CC, Zhan X. 1998. The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells. J. Biol. Chem. 273:25770-6
    • (1998) J. Biol. Chem. , vol.273 , pp. 25770-25776
    • Huang, C.1    Liu, J.2    Haudenchild, C.C.3    Zhan, X.4
  • 75
    • 0033565639 scopus 로고    scopus 로고
    • Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast
    • Huang KM, D'Hondt K, Riezman H, Lemmon SK. 1999. Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast. EMBO J. 18:3897-908
    • (1999) EMBO J. , vol.18 , pp. 3897-3908
    • Huang, K.M.1    D'Hondt, K.2    Riezman, H.3    Lemmon, S.K.4
  • 76
    • 0034795425 scopus 로고    scopus 로고
    • Endocytic protein intersectin-1 regulates actin assembly via Cdc42 and N-WASP
    • Hussain NK, Jenna S, Glogauer M, Quinn CC, Wasiak S, et al. 2001. Endocytic protein intersectin-1 regulates actin assembly via Cdc42 and N-WASP. Nat. Cell Biol. 3:927-32
    • (2001) Nat. Cell Biol. , vol.3 , pp. 927-932
    • Hussain, N.K.1    Jenna, S.2    Glogauer, M.3    Quinn, C.C.4    Wasiak, S.5
  • 77
    • 0032983521 scopus 로고    scopus 로고
    • Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells
    • Hussain NK, Yamabhai M, Ramjaun AR, Guy AM, Baranes D, et al. 1999. Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells. J Biol. Chem. 274:15671-77
    • (1999) J Biol. Chem. , vol.274 , pp. 15671-15677
    • Hussain, N.K.1    Yamabhai, M.2    Ramjaun, A.R.3    Guy, A.M.4    Baranes, D.5
  • 78
    • 0036856301 scopus 로고    scopus 로고
    • Cofilin, but not profilin, is required for Myosin-I-induced actin polymerization and the endocytic uptake in yeast
    • Idrissi FZ, Wolf BL, Geli MI. 2002. Cofilin, but not profilin, is required for Myosin-I-induced actin polymerization and the endocytic uptake in yeast. Mol. Biol. Cell 13:4074-87
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4074-4087
    • Idrissi, F.Z.1    Wolf, B.L.2    Geli, M.I.3
  • 79
    • 0027313677 scopus 로고
    • Dendritic cell progenitors phagocytose particulates, including bacillus Calmette-Guerin organisms, and sensitize mice to mycobacterial antigens in vivo
    • Inaba K, Inaba M, Naito M, Steinman RM. 1993. Dendritic cell progenitors phagocytose particulates, including bacillus Calmette-Guerin organisms, and sensitize mice to mycobacterial antigens in vivo. J. Exp. Med. 178:479-88
    • (1993) J. Exp. Med. , vol.178 , pp. 479-488
    • Inaba, K.1    Inaba, M.2    Naito, M.3    Steinman, R.M.4
  • 81
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis
    • Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. 2001. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 291:1047-51
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1    Koshiba, S.2    Kigawa, T.3    Kikuchi, A.4    Yokoyama, S.5    Takenawa, T.6
  • 83
    • 0022446007 scopus 로고
    • Down regulation of the α-factor pheromone receptor in S. cerevisiae
    • Jenness DD, Spatrick P. 1986. Down regulation of the α-factor pheromone receptor in S. cerevisiae. Cell 46:345-53
    • (1986) Cell , vol.46 , pp. 345-353
    • Jenness, D.D.1    Spatrick, P.2
  • 84
    • 0034496280 scopus 로고    scopus 로고
    • Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles
    • Kaksonen M, Peng HB, Rauvala H. 2000. Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles. J. Cell Sci. 113(Pt 24):4421-26
    • (2000) J. Cell Sci. , vol.113 , Issue.24 PART , pp. 4421-4426
    • Kaksonen, M.1    Peng, H.B.2    Rauvala, H.3
  • 85
    • 0030986659 scopus 로고    scopus 로고
    • HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain
    • Kalchman MA, Koide HB, McCutcheon K, Graham RK, Nichol K, et al. 1997. HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain. Nat. Genet. 16:44-53
    • (1997) Nat. Genet. , vol.16 , pp. 44-53
    • Kalchman, M.A.1    Koide, H.B.2    McCutcheon, K.3    Graham, R.K.4    Nichol, K.5
  • 86
    • 0036786951 scopus 로고    scopus 로고
    • Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae
    • Kaminska J, Gajewska B, Hopper AK, Zoladek T. 2002. Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 22:6946-48
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6946-6948
    • Kaminska, J.1    Gajewska, B.2    Hopper, A.K.3    Zoladek, T.4
  • 87
    • 0035966020 scopus 로고    scopus 로고
    • Insulin stimulates actin comet tails on intracellular GLUT4-containing compartments in differentiated 3T3L1 adipocytes
    • Kanzaki M, Watson RT, Khan AH, Pessin JE. 2001. Insulin stimulates actin comet tails on intracellular GLUT4-containing compartments in differentiated 3T3L1 adipocytes. J. Biol. Chem. 276:49331-36
    • (2001) J. Biol. Chem. , vol.276 , pp. 49331-49336
    • Kanzaki, M.1    Watson, R.T.2    Khan, A.H.3    Pessin, J.E.4
  • 88
    • 0033005568 scopus 로고    scopus 로고
    • Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery
    • Kay BK, Yamabhai M, Wendland B, Emr SD. 1999. Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery. Protein Sci. 8:435-38
    • (1999) Protein Sci. , vol.8 , pp. 435-438
    • Kay, B.K.1    Yamabhai, M.2    Wendland, B.3    Emr, S.D.4
  • 89
    • 0033980106 scopus 로고    scopus 로고
    • Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation
    • Kessels MM, Engqvist-Goldstein ÅE, Drubin DG. 2000. Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation. Mol. Biol. Cell 11:393-412
    • (2000) Mol. Biol. Cell , vol.11 , pp. 393-412
    • Kessels, M.M.1    Engqvist-Goldstein, Å.E.2    Drubin, D.G.3
  • 90
    • 0035897420 scopus 로고    scopus 로고
    • Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin
    • Kessels MM, Engqvist-Goldstein ÅE, Drubin DG, Qualmann B. 2001. Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin. J. Cell Biol. 153:351-66
    • (2001) J. Cell Biol. , vol.153 , pp. 351-366
    • Kessels, M.M.1    Engqvist-Goldstein, Å.E.2    Drubin, D.G.3    Qualmann, B.4
  • 91
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels MM, Qualmann B. 2002. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J. 21:6083-94
    • (2002) EMBO J. , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 92
    • 0024368508 scopus 로고
    • Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval
    • Koenig JH, Ikeda K. 1989. Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval. J. Neurosci. 9:3844-60
    • (1989) J. Neurosci. , vol.9 , pp. 3844-3860
    • Koenig, J.H.1    Ikeda, K.2
  • 93
    • 0020807636 scopus 로고
    • Reversible blockage of membrane retrieval and endocytosis in the garland cell of the temperature-sensitive mutant of Drosophila melanogaster, shibirets1
    • Kosaka T, Ikeda K. 1983. Reversible blockage of membrane retrieval and endocytosis in the garland cell of the temperature-sensitive mutant of Drosophila melanogaster, shibirets1. J. Cell Biol. 97:499-507
    • (1983) J. Cell Biol. , vol.97 , pp. 499-507
    • Kosaka, T.1    Ikeda, K.2
  • 94
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler E, Riezman H. 1993. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12:2855-62
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 96
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze C, Fujimoto LM, Yin HL, Schmid SL. 1997. The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J. Biol. Chem. 272:20332-35
    • (1997) J. Biol. Chem. , vol.272 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 97
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen P, Drubin DG. 1997. Cofilin promotes rapid actin filament turnover in vivo. Nature 388:78-82
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 98
    • 0032952693 scopus 로고    scopus 로고
    • SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors
    • Larbolette O, Wollscheid B, Schweikert J, Nielsen PJ, Wienands J. 1999. SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors. Mol. Cell. Biol. 19:1539-46
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1539-1546
    • Larbolette, O.1    Wollscheid, B.2    Schweikert, J.3    Nielsen, P.J.4    Wienands, J.5
  • 99
    • 0034707580 scopus 로고    scopus 로고
    • Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization
    • Lechler T, Shevchenko A, Li R. 2000. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. J. Cell Biol. 148:363-73
    • (2000) J. Cell Biol. , vol.148 , pp. 363-373
    • Lechler, T.1    Shevchenko, A.2    Li, R.3
  • 101
    • 0034645065 scopus 로고    scopus 로고
    • Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp
    • Lee WL, Bezanilla M, Pollard TD. 2000. Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp. J. Cell Biol. 151:789-800
    • (2000) J. Cell Biol. , vol.151 , pp. 789-800
    • Lee, W.L.1    Bezanilla, M.2    Pollard, T.D.3
  • 102
    • 0037205440 scopus 로고    scopus 로고
    • HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain
    • Legendre-Guillemin V, Metzler M, Charbonneau M, Gan L, Chopra V, et al. 2002. HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain. J. Biol. Chem. 277:19897-904
    • (2002) J. Biol. Chem. , vol.277 , pp. 19897-19904
    • Legendre-Guillemin, V.1    Metzler, M.2    Charbonneau, M.3    Gan, L.4    Chopra, V.5
  • 103
    • 0035936557 scopus 로고    scopus 로고
    • Clathrin uncoating: Auxilin comes to life
    • Lemmon SK. 2001. Clathrin uncoating: auxilin comes to life. Curr. Biol. 11:R49-52
    • (2001) Curr. Biol. , vol.11
    • Lemmon, S.K.1
  • 104
    • 0037201064 scopus 로고    scopus 로고
    • Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p
    • Li H, Page N, Bussey H. 2002. Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth to daughter cells and interact with cis-Golgi protein Kre6p. Yeast 19:1097-112
    • (2002) Yeast , vol.19 , pp. 1097-1112
    • Li, H.1    Page, N.2    Bussey, H.3
  • 105
    • 0031045512 scopus 로고    scopus 로고
    • Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton
    • Li R. 1997. Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J. Cell Biol. 136:649-58
    • (1997) J. Cell Biol. , vol.136 , pp. 649-658
    • Li, R.1
  • 106
    • 0028871169 scopus 로고
    • Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast
    • Li R, Zheng Y, Drubin DG. 1995. Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. J. Cell Biol. 128:599-615
    • (1995) J. Cell Biol. , vol.128 , pp. 599-615
    • Li, R.1    Zheng, Y.2    Drubin, D.G.3
  • 107
    • 0037155857 scopus 로고    scopus 로고
    • The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation
    • Lin Q, Lo CG, Cerione RA, Yang W. 2002. The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation. J. Biol. Chem. 277:10134-38
    • (2002) J. Biol. Chem. , vol.277 , pp. 10134-10138
    • Lin, Q.1    Lo, C.G.2    Cerione, R.A.3    Yang, W.4
  • 108
    • 0032480013 scopus 로고    scopus 로고
    • A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate
    • Lock P, Abram CL, Gibson T, Courtneidge SA. 1998. A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate. EMBO J. 17:4346-57
    • (1998) EMBO J. , vol.17 , pp. 4346-4357
    • Lock, P.1    Abram, C.L.2    Gibson, T.3    Courtneidge, S.A.4
  • 109
    • 0034192223 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein is necessary for efficient IgG-mediated phagocytosis
    • Lorenzi R, Brickell PM, Katz DR, Kinnon C, Thrasher AJ. 2000. Wiskott-Aldrich syndrome protein is necessary for efficient IgG-mediated phagocytosis. Blood 95:2943-46
    • (2000) Blood , vol.95 , pp. 2943-2946
    • Lorenzi, R.1    Brickell, P.M.2    Katz, D.R.3    Kinnon, C.4    Thrasher, A.J.5
  • 110
    • 0032835492 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex
    • Madania A, Dumoulin P, Grava S, Kitamoto H, Scharer-Brodbeck C, et al. 1999. The Saccharomyces cerevisiae homologue of human Wiskott-Aldrich syndrome protein Las17p interacts with the Arp2/3 complex. Mol. Biol. Cell 10:3521-38
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3521-3538
    • Madania, A.1    Dumoulin, P.2    Grava, S.3    Kitamoto, H.4    Scharer-Brodbeck, C.5
  • 111
    • 0036443534 scopus 로고    scopus 로고
    • Conserved features of endocytosis in Dictyostelium
    • Maniak M. 2002. Conserved features of endocytosis in Dictyostelium. Int. Rev. Cytol. 221:257-87
    • (2002) Int. Rev. Cytol. , vol.221 , pp. 257-287
    • Maniak, M.1
  • 112
    • 0035067475 scopus 로고    scopus 로고
    • Phagocytosis and the actin cytoskeleton
    • May RC, Machesky LM. 2001. Phagocytosis and the actin cytoskeleton. J. Cell Sci. 114: 1061-77
    • (2001) J. Cell Sci. , vol.114 , pp. 1061-1077
    • May, R.C.1    Machesky, L.M.2
  • 113
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann RO, Craig SW. 1997. The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Natl. Acad. Sci. USA 94:5679-84
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 114
    • 0033539916 scopus 로고    scopus 로고
    • Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein: Actin interaction
    • McCann RO, Craig SW. 1999. Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein: actin interaction. Biochem. Biophys. Res. Commun. 266:135-40
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 135-140
    • McCann, R.O.1    Craig, S.W.2
  • 115
    • 0035905308 scopus 로고    scopus 로고
    • The intersectin 2 adaptor links Wiskott Aldrich Syndrome protein (WASp)-mediated actin polymerization to T cell antigen receptor endocytosis
    • McGavin MK, Badour K, Hardy LA, Kubiseski TJ, Zhang J, Siminovitch KA. 2001. The intersectin 2 adaptor links Wiskott Aldrich Syndrome protein (WASp)-mediated actin polymerization to T cell antigen receptor endocytosis. J. Exp. Med. 194:1777-87
    • (2001) J. Exp. Med. , vol.194 , pp. 1777-1787
    • McGavin, M.K.1    Badour, K.2    Hardy, L.A.3    Kubiseski, T.J.4    Zhang, J.5    Siminovitch, K.A.6
  • 116
    • 0033529056 scopus 로고    scopus 로고
    • Endocytosis: An assembly protein for clathrin cages
    • McMahon HT. 1999. Endocytosis: an assembly protein for clathrin cages. Curr. Biol. 9:R332-35
    • (1999) Curr. Biol. , vol.9
    • McMahon, H.T.1
  • 117
    • 0034597062 scopus 로고    scopus 로고
    • Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape
    • McNiven MA, Kim L, Krueger EW, Orth JD, Cao H, Wong TW. 2000. Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape. J. Cell Biol. 151:187-98
    • (2000) J. Cell Biol. , vol.151 , pp. 187-198
    • McNiven, M.A.1    Kim, L.2    Krueger, E.W.3    Orth, J.D.4    Cao, H.5    Wong, T.W.6
  • 118
    • 0036633295 scopus 로고    scopus 로고
    • The endocytic machinery at an interface with the actin cytoskeleton: A dynamic, hip intersection
    • McPherson PS. 2002. The endocytic machinery at an interface with the actin cytoskeleton: a dynamic, hip intersection. Trends Cell Biol. 12:312-15
    • (2002) Trends Cell Biol. , vol.12 , pp. 312-315
    • McPherson, P.S.1
  • 119
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield CJ, Feldman ME, Wan L, Almers W. 2002. Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat. Cell Biol. 4:691-98
    • (2002) Nat. Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 121
    • 0035914402 scopus 로고    scopus 로고
    • HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2
    • Metzler M, Legendre-Guillemin V, Gan L, Chopra V, Kwok A, et al. 2001. HIP1 functions in clathrin-mediated endocytosis through binding to clathrin and adaptor protein 2. J. Biol. Chem. 276:39271-76
    • (2001) J. Biol. Chem. , vol.276 , pp. 39271-39276
    • Metzler, M.1    Legendre-Guillemin, V.2    Gan, L.3    Chopra, V.4    Kwok, A.5
  • 122
    • 0033544964 scopus 로고    scopus 로고
    • A requirement for ankyrin binding to clathrin during coated pit budding
    • Michaely P, Kamal A, Anderson RG, Bennett V. 1999. A requirement for ankyrin binding to clathrin during coated pit budding. J. Biol. Chem. 274:35908-13
    • (1999) J. Biol. Chem. , vol.274 , pp. 35908-35913
    • Michaely, P.1    Kamal, A.2    Anderson, R.G.3    Bennett, V.4
  • 123
    • 0037436305 scopus 로고    scopus 로고
    • Mammalian actin binding protein 1 is essential for endocytosis but not lamellipodia formation: Functional analysis by RNA interference
    • Mise-Omata S, Montagne B, Deckert M, Wienands J, Acuto O. 2003. Mammalian actin binding protein 1 is essential for endocytosis but not lamellipodia formation: functional analysis by RNA interference. Biochem. Biophys. Res. Commun. 301:704-10
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 704-710
    • Mise-Omata, S.1    Montagne, B.2    Deckert, M.3    Wienands, J.4    Acuto, O.5
  • 124
    • 0035824673 scopus 로고    scopus 로고
    • Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins
    • Mishra SK, Agostinelli NR, Brett TJ, Mizukami I, Ross TS, Traub LM. 2001. Clathrin-and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins. J. Biol. Chem. 276:46230-36
    • (2001) J. Biol. Chem. , vol.276 , pp. 46230-46236
    • Mishra, S.K.1    Agostinelli, N.R.2    Brett, T.J.3    Mizukami, I.4    Ross, T.S.5    Traub, L.M.6
  • 125
    • 0034503124 scopus 로고    scopus 로고
    • All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis
    • Modregger J, Ritter B, Witter B, Paulsson M, Plomann M. 2000. All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. J. Cell Sci. 113(Pt 24):4511-21
    • (2000) J. Cell Sci. , vol.113 , Issue.24 PT , pp. 4511-4521
    • Modregger, J.1    Ritter, B.2    Witter, B.3    Paulsson, M.4    Plomann, M.5
  • 126
    • 0030813921 scopus 로고    scopus 로고
    • The yeast actin-related protein Arp2p is required for the internalization step of endocytosis
    • Moreau V, Galán JM, Devilliers G, Haguenauer-Tsapis R, Winsor B. 1997. The yeast actin-related protein Arp2p is required for the internalization step of endocytosis. Mol. Biol. Cell 8:1361-75
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1361-1375
    • Moreau, V.1    Galán, J.M.2    Devilliers, G.3    Haguenauer-Tsapis, R.4    Winsor, B.5
  • 127
    • 0029959468 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton
    • Moreau V, Madania A, Martin RP, Winson B. 1996. The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134:117-32
    • (1996) J. Cell Biol. , vol.134 , pp. 117-132
    • Moreau, V.1    Madania, A.2    Martin, R.P.3    Winson, B.4
  • 128
    • 0036242467 scopus 로고    scopus 로고
    • Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton
    • Morris SM, Arden SD, Roberts RC, Kendrick-Jones J, Cooper JA, et al. 2002. Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton. Traffic 3:331-41
    • (2002) Traffic , vol.3 , pp. 331-341
    • Morris, S.M.1    Arden, S.D.2    Roberts, R.C.3    Kendrick-Jones, J.4    Cooper, J.A.5
  • 129
    • 0035099375 scopus 로고    scopus 로고
    • Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2
    • Morris SM, Cooper JA. 2001. Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2. Traffic 2:111-23
    • (2001) Traffic , vol.2 , pp. 111-123
    • Morris, S.M.1    Cooper, J.A.2
  • 131
    • 0028204439 scopus 로고
    • Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane
    • Mulholland J, Preuss D, Moon A, Wong A, Drubin D, Botstein D. 1994. Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J. Cell Biol. 125:381-91
    • (1994) J. Cell Biol. , vol.125 , pp. 381-391
    • Mulholland, J.1    Preuss, D.2    Moon, A.3    Wong, A.4    Drubin, D.5    Botstein, D.6
  • 132
    • 0030930123 scopus 로고    scopus 로고
    • Yeast actin cytoskeleton mutants accumulate anew class of Golgi-derived secretary vesicle
    • Mulholland J, Wesp A, Riezman H, Botstein D. 1997. Yeast actin cytoskeleton mutants accumulate anew class of Golgi-derived secretary vesicle. Mol. Biol. Cell 8:1481-99
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1481-1499
    • Mulholland, J.1    Wesp, A.2    Riezman, H.3    Botstein, D.4
  • 133
    • 0035952983 scopus 로고    scopus 로고
    • Molecular requirements for the internalisation step of endocytosis: Insights from yeast
    • Munn AL. 2001. Molecular requirements for the internalisation step of endocytosis: insights from yeast. Biochim. Biophys. Acta 1535:236-57
    • (2001) Biochim. Biophys. Acta , vol.1535 , pp. 236-257
    • Munn, A.L.1
  • 135
    • 0027997975 scopus 로고
    • Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: Identification of six new END genes
    • Munn AL, Riezman H. 1994. Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: identification of six new END genes. J. Cell Biol. 127:373-86
    • (1994) J. Cell Biol. , vol.127 , pp. 373-386
    • Munn, A.L.1    Riezman, H.2
  • 136
    • 0028856410 scopus 로고
    • end5, end6, and end7: Mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae
    • Munn AL, Stevenson BJ, Geli MI, Riezman H. 1995. end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 6:1721-42
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1721-1742
    • Munn, A.L.1    Stevenson, B.J.2    Geli, M.I.3    Riezman, H.4
  • 137
    • 0032572759 scopus 로고    scopus 로고
    • The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast
    • Naqvi SN, Zahn R, Mitchell DA, Stevenson BJ, Munn AL. 1998. The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast. Curr. Biol. 8:959-62
    • (1998) Curr. Biol. , vol.8 , pp. 959-962
    • Naqvi, S.N.1    Zahn, R.2    Mitchell, D.A.3    Stevenson, B.J.4    Munn, A.L.5
  • 138
    • 0034687237 scopus 로고    scopus 로고
    • Dendritic cells: New roles for Cdc42 and Rac in antigen uptake?
    • Nobes C, Marsh M. 2000. Dendritic cells: new roles for Cdc42 and Rac in antigen uptake? Curr. Biol. 10:R739-41
    • (2000) Curr. Biol. , vol.10
    • Nobes, C.1    Marsh, M.2
  • 139
    • 0034710252 scopus 로고    scopus 로고
    • A functional link between dynamin and the actin cytoskeleton at podosomes
    • Ochoa GC, Slepnev VI, Neff L, Ringstad N, Takei K, et al. 2000. A functional link between dynamin and the actin cytoskeleton at podosomes. J. Cell Biol. 150:377-89
    • (2000) J. Cell Biol. , vol.150 , pp. 377-389
    • Ochoa, G.C.1    Slepnev, V.I.2    Neff, L.3    Ringstad, N.4    Takei, K.5
  • 140
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh P, McIntosh DP, Schnitzer JE. 1998. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 141:101-14
    • (1998) J. Cell Biol. , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 141
    • 0035921432 scopus 로고    scopus 로고
    • Abp1p and cortactin, new "hand-holds" for actin
    • Olazabal IM, Machesky LM. 2001. Abp1p and cortactin, new "hand-holds" for actin. J. Cell Biol. 154:679-82
    • (2001) J. Cell Biol. , vol.154 , pp. 679-682
    • Olazabal, I.M.1    Machesky, L.M.2
  • 142
    • 0037039414 scopus 로고    scopus 로고
    • The large GTPase dynamin regulates actin comet formation and movement in living cells
    • Orth JD, Krueger EW, Cao H, McNiven MA. 2002. The large GTPase dynamin regulates actin comet formation and movement in living cells. Proc. Natl. Acad. Sci. USA 99:167-72
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 167-172
    • Orth, J.D.1    Krueger, E.W.2    Cao, H.3    McNiven, M.A.4
  • 145
    • 0023891818 scopus 로고
    • Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast
    • Payne GS, Baker D, van Tuinen E, Schekman R. 1988. Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast. J. Cell Biol. 106:1453-61
    • (1988) J. Cell Biol. , vol.106 , pp. 1453-1461
    • Payne, G.S.1    Baker, D.2    Van Tuinen, E.3    Schekman, R.4
  • 146
    • 0036239115 scopus 로고    scopus 로고
    • Endocytosis via caveolae
    • Pelkmans L, Helenius A. 2002. Endocytosis via caveolae. Traffic 3:311-20
    • (2002) Traffic , vol.3 , pp. 311-320
    • Pelkmans, L.1    Helenius, A.2
  • 147
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L, Puntener D, Helenius A. 2002. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 296:535-39
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 148
    • 0034056057 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast
    • Pruyne D, Bretscher A. 2000a. Polarization of cell growth in yeast. J. Cell Sci. 113(Pt 4): 571-85
    • (2000) J. Cell Sci. , vol.113 , Issue.4 PART , pp. 571-585
    • Pruyne, D.1    Bretscher, A.2
  • 149
    • 0034002965 scopus 로고    scopus 로고
    • Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states
    • Pruyne D, Bretscher A. 2000b. Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states. J. Cell Sci. 113(Pt 3):365-75
    • (2000) J. Cell Sci. , vol.113 , Issue.3 PART , pp. 365-375
    • Pruyne, D.1    Bretscher, A.2
  • 150
    • 0034611006 scopus 로고    scopus 로고
    • Syndapin isoforms participate in receptor-mediated endocytosis and actin organization
    • Qualmann B, Kelly RB. 2000. Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J. Cell Biol. 148:1047-62
    • (2000) J. Cell Biol. , vol.148 , pp. 1047-1062
    • Qualmann, B.1    Kelly, R.B.2
  • 151
  • 152
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I, a synaptic dynaminbinding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann B, Roos J, DiGregorio PJ, Kelly RB. 1999. Syndapin I, a synaptic dynaminbinding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell 10:501-13
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 153
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths S, Rohrer J, Crausaz F, Riezman H. 1993. end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120:55-65
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 154
    • 0035890289 scopus 로고    scopus 로고
    • Caveolins and caveolae: Molecular and functional relationships
    • Razani B, Lisanti MP. 2001. Caveolins and caveolae: molecular and functional relationships. Exp. Cell Res. 271:36-44
    • (2001) Exp. Cell Res. , vol.271 , pp. 36-44
    • Razani, B.1    Lisanti, M.P.2
  • 155
    • 0024294018 scopus 로고
    • The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain
    • Reneke JE, Blumer KJ, Courchesne WE, Thorner J. 1988. The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain. Cell 55:221-34
    • (1988) Cell , vol.55 , pp. 221-234
    • Reneke, J.E.1    Blumer, K.J.2    Courchesne, W.E.3    Thorner, J.4
  • 156
    • 0021929527 scopus 로고
    • Endocytosis in yeast: Several of the yeast secretory mutants are defective in endocytosis
    • Riezman H. 1985. Endocytosis in yeast: several of the yeast secretory mutants are defective in endocytosis. Cell 40:1001-9
    • (1985) Cell , vol.40 , pp. 1001-1009
    • Riezman, H.1
  • 157
    • 0033199465 scopus 로고    scopus 로고
    • Endophilin/SH3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis
    • Ringstad N, Gad H, Low P, Di Paolo G, Brodin L, et al. 1999. Endophilin/SH3p4 is required for the transition from early to late stages in clathrin-mediated synaptic vesicle endocytosis. Neuron 24:143-54
    • (1999) Neuron , vol.24 , pp. 143-154
    • Ringstad, N.1    Gad, H.2    Low, P.3    Di Paolo, G.4    Brodin, L.5
  • 158
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R, Ma L, Miki H, Lopez M, Kirchhausen T, et al. 1999. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97:221-31
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5
  • 159
    • 0027207946 scopus 로고
    • Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-pheromone receptor in yeast
    • Rohrer J, Benedetti H, Zanolari B, Riezman H. 1993. Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-pheromone receptor in yeast. Mol. Biol. Cell 4:511-21
    • (1993) Mol. Biol. Cell , vol.4 , pp. 511-521
    • Rohrer, J.1    Benedetti, H.2    Zanolari, B.3    Riezman, H.4
  • 160
    • 0032563187 scopus 로고    scopus 로고
    • Dap160, a neural-specific Eps 15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin
    • Roos J, Kelly RB. 1998. Dap160, a neural-specific Eps 15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin. J. Biol. Chem. 273: 19108-19
    • (1998) J. Biol. Chem. , vol.273 , pp. 19108-19119
    • Roos, J.1    Kelly, R.B.2
  • 161
    • 0033518315 scopus 로고    scopus 로고
    • The endocytic machinery in nerve terminals surrounds sites of exocytosis
    • Roos J, Kelly RB. 1999. The endocytic machinery in nerve terminals surrounds sites of exocytosis. Curr. Biol. 9:1411-14
    • (1999) Curr. Biol. , vol.9 , pp. 1411-1414
    • Roos, J.1    Kelly, R.B.2
  • 163
    • 17144439652 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3
    • Rozelle AL, Machesky LM, Yamamoto M, Driessens MH, Insall RH, et al. 2000. Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2/3. Curr. Biol. 10:311-20
    • (2000) Curr. Biol. , vol.10 , pp. 311-320
    • Rozelle, A.L.1    Machesky, L.M.2    Yamamoto, M.3    Driessens, M.H.4    Insall, R.H.5
  • 164
    • 0019068962 scopus 로고
    • Role of coated vesicles, microfilaments, and calmodulin in receptor-mediated endocytosis by cultured B lymphoblastoid cells
    • Salisbury JL, Condeelis JS, Satir P. 1980. Role of coated vesicles, microfilaments, and calmodulin in receptor-mediated endocytosis by cultured B lymphoblastoid cells. J. Cell Biol. 87:132-41
    • (1980) J. Cell Biol. , vol.87 , pp. 132-141
    • Salisbury, J.L.1    Condeelis, J.S.2    Satir, P.3
  • 165
    • 0029148878 scopus 로고
    • Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products
    • Sallusto F, Cella M, Danieli C, Lanzavecchia A. 1995. Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: downregulation by cytokines and bacterial products. J. Exp. Med. 182:389-400
    • (1995) J. Exp. Med. , vol.182 , pp. 389-400
    • Sallusto, F.1    Cella, M.2    Danieli, C.3    Lanzavecchia, A.4
  • 166
    • 0025259884 scopus 로고
    • Selective modulation of the endocytic uptake of ricin and fluid phase markers without alteration in transferrin endocytosis
    • Sandvig K, van Deurs B. 1990. Selective modulation of the endocytic uptake of ricin and fluid phase markers without alteration in transferrin endocytosis. J. Biol. Chem. 265:6382-88
    • (1990) J. Biol. Chem. , vol.265 , pp. 6382-6388
    • Sandvig, K.1    Van Deurs, B.2
  • 167
    • 0036797206 scopus 로고    scopus 로고
    • A glimpse of coated vesicle creation? Well almost!
    • Santini F, Keen JH. 2002. A glimpse of coated vesicle creation? Well almost! Nat. Cell Biol. 4:E230-32
    • (2002) Nat. Cell Biol. , vol.4
    • Santini, F.1    Keen, J.H.2
  • 168
    • 0036468381 scopus 로고    scopus 로고
    • Coupling actin dynamics and membrane dynamics during endocytosis
    • Schafer DA. 2002. Coupling actin dynamics and membrane dynamics during endocytosis. Curr. Opin. Cell Biol. 14:76-81
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 76-81
    • Schafer, D.A.1
  • 169
  • 171
    • 0025917331 scopus 로고
    • Stage-specific assays for coated pit formation and coated vesicle budding in vitro
    • Schmid SL, Smythe E. 1991. Stage-specific assays for coated pit formation and coated vesicle budding in vitro. J. Cell Biol. 114:869-80
    • (1991) J. Cell Biol. , vol.114 , pp. 869-880
    • Schmid, S.L.1    Smythe, E.2
  • 172
    • 0033539120 scopus 로고    scopus 로고
    • Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid
    • Schmidt A, Wolde M, Thiele C, Fest W, Kratzin H, et al. 1999. Endophilin I mediates synaptic vesicle formation by transfer of arachidonate to lysophosphatidic acid. Nature 401:133-41
    • (1999) Nature , vol.401 , pp. 133-141
    • Schmidt, A.1    Wolde, M.2    Thiele, C.3    Fest, W.4    Kratzin, H.5
  • 173
    • 0027211848 scopus 로고
    • The product of the EMS1 gene, amplified and overexpressed in human carcinomas, is homologous to a v-src substrate and is located in cell-substratum contact sites
    • Schuuring E, Verhoeven E, Litvinov S, Michalides RJ. 1993. The product of the EMS1 gene, amplified and overexpressed in human carcinomas, is homologous to a v-src substrate and is located in cell-substratum contact sites. Mol. Cell. Biol. 13:2891-98
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2891-2898
    • Schuuring, E.1    Verhoeven, E.2    Litvinov, S.3    Michalides, R.J.4
  • 174
    • 0034909964 scopus 로고    scopus 로고
    • The WASp-like protein scar regulates macropinocytosis, phagocytosis and endosomal membrane flow in Dictyostelium
    • Seastone DJ, Harris E, Temesvari LA, Bear JE, Saxe CL, Cardelli J. 2001. The WASp-like protein scar regulates macropinocytosis, phagocytosis and endosomal membrane flow in Dictyostelium. J. Cell Sci. 114:2673-83
    • (2001) J. Cell Sci. , vol.114 , pp. 2673-2683
    • Seastone, D.J.1    Harris, E.2    Temesvari, L.A.3    Bear, J.E.4    Saxe, C.L.5    Cardelli, J.6
  • 175
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: A diverse superfamily
    • Sellers JR. 2000. Myosins: a diverse superfamily. Biochim. Biophys. Acta 1496:3-22
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 176
    • 0033106167 scopus 로고    scopus 로고
    • The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
    • Sengar AS, Wang W, Bishay J, Cohen S, Egan SE. 1999. The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15. EMBO J. 18:1159-71
    • (1999) EMBO J. , vol.18 , pp. 1159-1171
    • Sengar, A.S.1    Wang, W.2    Bishay, J.3    Cohen, S.4    Egan, S.E.5
  • 177
    • 0034189032 scopus 로고    scopus 로고
    • Garrotes, springs, ratchets, and whips: Putting dynamin models to the test
    • Sever S, Damke H, Schmid SL. 2000. Garrotes, springs, ratchets, and whips: putting dynamin models to the test. Traffic 1:385-92
    • (2000) Traffic , vol.1 , pp. 385-392
    • Sever, S.1    Damke, H.2    Schmid, S.L.3
  • 179
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih SC, Katzmann DJ, Schnell JD, Sutanto M, Emr SD, Hicke L. 2002. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4:389-93
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 180
    • 0034677207 scopus 로고    scopus 로고
    • Monoubiquitin carries a novel internalization signal that is appended to activated receptors
    • Shih SC, Sloper-Mould KE, Hicke L. 2000. Monoubiquitin carries a novel internalization signal that is appended to activated receptors. EMBO J. 19:187-98
    • (2000) EMBO J. , vol.19 , pp. 187-198
    • Shih, S.C.1    Sloper-Mould, K.E.2    Hicke, L.3
  • 181
    • 0037195182 scopus 로고    scopus 로고
    • Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton
    • Shupliakov O, Bloom O, Gustafsson JS, Kjaerulff O, Low P, et al. 2002. Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. Proc. Natl. Acad. Sci. USA 99:14476-81
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14476-14481
    • Shupliakov, O.1    Bloom, O.2    Gustafsson, J.S.3    Kjaerulff, O.4    Low, P.5
  • 183
    • 0033147449 scopus 로고    scopus 로고
    • SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation
    • Simpson F, Hussain NK, Qualmann B, Kelly RB, Kay BK, et al. 1999. SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation. Nat. Cell Biol. 1:119-24
    • (1999) Nat. Cell Biol. , vol.1 , pp. 119-124
    • Simpson, F.1    Hussain, N.K.2    Qualmann, B.3    Kelly, R.B.4    Kay, B.K.5
  • 184
    • 0345646448 scopus 로고    scopus 로고
    • Synaptojanin family members are implicated in endocytic membrane traffic in yeast
    • Singer-Kruger B, Nemoto Y, Daniell L, FerroNovick S, De Camilli P. 1998. Synaptojanin family members are implicated in endocytic membrane traffic in yeast. J. Cell Sci. 111(Pt 22):3347-56
    • (1998) J. Cell Sci. , vol.111 , Issue.22 PART , pp. 3347-3356
    • Singer-Kruger, B.1    Nemoto, Y.2    Daniell, L.3    Ferronovick, S.4    De Camilli, P.5
  • 185
    • 0035023988 scopus 로고    scopus 로고
    • The life cycle of actin patches in mating yeast
    • Smith MG, Swamy SR, Pon LA. 2001. The life cycle of actin patches in mating yeast. J. Cell Sci. 114:1505-13
    • (2001) J. Cell Sci. , vol.114 , pp. 1505-1513
    • Smith, M.G.1    Swamy, S.R.2    Pon, L.A.3
  • 186
    • 0030686464 scopus 로고    scopus 로고
    • Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape, and osmohomeostasis
    • Srinivasan S, Seaman M, Nemoto Y, Daniell L, Suchy SF, et al. 1997. Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape, and osmohomeostasis. Eur. J. Cell Biol. 74:350-60
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 350-360
    • Srinivasan, S.1    Seaman, M.2    Nemoto, Y.3    Daniell, L.4    Suchy, S.F.5
  • 187
    • 0027752442 scopus 로고
    • Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast
    • Tan PK, Davis NG, Sprague GF, Payne GS. 1993. Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast. J. Cell Biol. 123:1707-16
    • (1993) J. Cell Biol. , vol.123 , pp. 1707-1716
    • Tan, P.K.1    Davis, N.G.2    Sprague, G.F.3    Payne, G.S.4
  • 188
    • 0030459065 scopus 로고    scopus 로고
    • The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae
    • Tan PK, Howard JP, Payne GS. 1996. The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae. J. Cell Biol. 135:1789-800
    • (1996) J. Cell Biol. , vol.135 , pp. 1789-1800
    • Tan, P.K.1    Howard, J.P.2    Payne, G.S.3
  • 189
    • 0029772320 scopus 로고    scopus 로고
    • The EH-domain-containing protein Pan1 is required for normal
    • Tang HY, Cai M. 1996. The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:4897-914
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4897-4914
    • Tang, H.Y.1    Cai, M.2
  • 190
    • 0344279906 scopus 로고    scopus 로고
    • EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae
    • Tang HY, Munn A, Cai M. 1997. EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:4294-304
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4294-4304
    • Tang, H.Y.1    Munn, A.2    Cai, M.3
  • 191
    • 0033622305 scopus 로고    scopus 로고
    • Pan1p, End3p, and Slalp, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis
    • Tang HY, Xu J, Cai M. 2000. Pan1p, End3p, and Slalp, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis. Mol. Cell. Biol. 20:12-25
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 12-25
    • Tang, H.Y.1    Xu, J.2    Cai, M.3
  • 192
    • 0034614930 scopus 로고    scopus 로고
    • Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP
    • Taunton J, Rowning BA, Coughlin ML, Wu M, Moon RT, et al. 2000. Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP. J. Cell Biol. 148: 519-30
    • (2000) J. Cell Biol. , vol.148 , pp. 519-530
    • Taunton, J.1    Rowning, B.A.2    Coughlin, M.L.3    Wu, M.4    Moon, R.T.5
  • 193
    • 0035947607 scopus 로고    scopus 로고
    • The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors
    • Teo M, Tan L, Lim L, Manser E. 2001. The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors. J. Biol. Chem. 276:18392-98
    • (2001) J. Biol. Chem. , vol.276 , pp. 18392-18398
    • Teo, M.1    Tan, L.2    Lim, L.3    Manser, E.4
  • 194
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell J, Shih S, Dunn R, Hicke L. 1998. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell 1:193-202
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 195
    • 0036151510 scopus 로고    scopus 로고
    • Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking
    • Thomsen P, Roepstorff K, Stahlhut M, van Deurs B. 2002. Caveolae are highly immobile plasma membrane microdomains, which are not involved in constitutive endocytic trafficking. Mol. Biol. Cell 13:238-50
    • (2002) Mol. Biol. Cell , vol.13 , pp. 238-250
    • Thomsen, P.1    Roepstorff, K.2    Stahlhut, M.3    Van Deurs, B.4
  • 196
    • 0034703049 scopus 로고    scopus 로고
    • Intersectin can regulate the Ras/MAP kinase pathway independent of its role in endocytosis
    • Tong XK, Hussain NK, Adams AG, O'Bryan JP, McPherson PS. 2000. Intersectin can regulate the Ras/MAP kinase pathway independent of its role in endocytosis. J. Biol. Chem. 275:29894-99
    • (2000) J. Biol. Chem. , vol.275 , pp. 29894-29899
    • Tong, X.K.1    Hussain, N.K.2    Adams, A.G.3    O'Bryan, J.P.4    McPherson, P.S.5
  • 197
    • 0035090317 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-mediated actin polymerization by cortactin
    • Uruno T, Liu J, Zhang P, Fan Y, Egile C, et al. 2001. Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nat. Cell. Biol. 3:259-66
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 259-266
    • Uruno, T.1    Liu, J.2    Zhang, P.3    Fan, Y.4    Egile, C.5
  • 198
    • 0031416482 scopus 로고    scopus 로고
    • Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton
    • Vaduva G, Martin NC, Hopper AK. 1997. Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J. Cell Biol. 139:1821-33
    • (1997) J. Cell Biol. , vol.139 , pp. 1821-1833
    • Vaduva, G.1    Martin, N.C.2    Hopper, A.K.3
  • 200
    • 0035880457 scopus 로고    scopus 로고
    • The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis
    • Waelter S, Scherzinger E, Hasenbank R, Nordhoff E, Lurz R, et al. 2001. The huntingtin interacting protein HIP1 is a clathrin and alpha-adaptin-binding protein involved in receptor-mediated endocytosis. Hum. Mol. Genet. 10:1807-17
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1807-1817
    • Waelter, S.1    Scherzinger, E.2    Hasenbank, R.3    Nordhoff, E.4    Lurz, R.5
  • 201
  • 202
    • 0037089086 scopus 로고    scopus 로고
    • Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics
    • Warren DT, Andrews PD, Gourlay CW, Ayscough KR. 2002. Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics. J. Cell Sci. 115:1703-15
    • (2002) J. Cell Sci. , vol.115 , pp. 1703-1715
    • Warren, D.T.1    Andrews, P.D.2    Gourlay, C.W.3    Ayscough, K.R.4
  • 203
    • 0035854813 scopus 로고    scopus 로고
    • The Ras/Rac guanine nucleotide exchange factor mammalian Son-of-sevenless interacts with PAC-SIN 1/syndapin I, a regulator of endocytosis and the actin cytoskeleton
    • Wasiak S, Quinn CC, Ritter B, de Heuvel E, Baranes D, et al. 2001. The Ras/Rac guanine nucleotide exchange factor mammalian Son-of-sevenless interacts with PAC-SIN 1/syndapin I, a regulator of endocytosis and the actin cytoskeleton. J. Biol. Chem. 276:26622-28
    • (2001) J. Biol. Chem. , vol.276 , pp. 26622-26628
    • Wasiak, S.1    Quinn, C.C.2    Ritter, B.3    De Heuvel, E.4    Baranes, D.5
  • 204
    • 0035196516 scopus 로고    scopus 로고
    • In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation
    • Watson HA, Cope MJ, Groen AC, Drubin DG, Wendland B. 2001. In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Mol. Biol. Cell 12:3668-79
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3668-3679
    • Watson, H.A.1    Cope, M.J.2    Groen, A.C.3    Drubin, D.G.4    Wendland, B.5
  • 205
    • 0035814938 scopus 로고    scopus 로고
    • Cortactin promotes and stabilizes Arp2/3-induced actin filament network formation
    • Weaver AM, Karginov AV, Kinley AW, Weed SA, Li Y, et al. 2001. Cortactin promotes and stabilizes Arp2/3-induced actin filament network formation. Curr. Biol. 11:370-74
    • (2001) Curr. Biol. , vol.11 , pp. 370-374
    • Weaver, A.M.1    Karginov, A.V.2    Kinley, A.W.3    Weed, S.A.4    Li, Y.5
  • 207
    • 0033619258 scopus 로고    scopus 로고
    • Myosin VI is an actin-based motor that moves backwards
    • Wells AL, Lin AW, Chen LQ, Safer D, Cain SM, et al. 1999. Myosin VI is an actin-based motor that moves backwards. Nature 401:505-8
    • (1999) Nature , vol.401 , pp. 505-508
    • Wells, A.L.1    Lin, A.W.2    Chen, L.Q.3    Safer, D.4    Cain, S.M.5
  • 208
    • 0036902815 scopus 로고    scopus 로고
    • Epsins: Adaptors in endocytosis?
    • Wendland B. 2002. Epsins: adaptors in endocytosis? Nat. Rev. Mol. Cell Biol. 3:971-77
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 971-977
    • Wendland, B.1
  • 209
    • 0032489873 scopus 로고    scopus 로고
    • Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis
    • Wendland B, Emr SD. 1998. Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis. J. Cell Biol. 141:71-84
    • (1998) J. Cell Biol. , vol.141 , pp. 71-84
    • Wendland, B.1    Emr, S.D.2
  • 210
    • 12644263389 scopus 로고    scopus 로고
    • A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15
    • Wendland B, McCaffery JM, Xiao Q, Emr SD. 1996. A novel fluorescence-activated cell sorter-based screen for yeast endocytosis mutants identifies a yeast homologue of mammalian eps15. J. Cell Biol. 135:1485-500
    • (1996) J. Cell Biol. , vol.135 , pp. 1485-1500
    • Wendland, B.1    McCaffery, J.M.2    Xiao, Q.3    Emr, S.D.4
  • 211
    • 0033575748 scopus 로고    scopus 로고
    • Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis
    • Wendland B, Steece KE, Emr SD. 1999. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 18:4383-93
    • (1999) EMBO J. , vol.18 , pp. 4383-4393
    • Wendland, B.1    Steece, K.E.2    Emr, S.D.3
  • 212
    • 0030785341 scopus 로고    scopus 로고
    • End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae
    • Wesp A, Hicke L, Palecek J, Lombardi R, Aust T, et al. 1997. End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 8:2291-306
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2291-2306
    • Wesp, A.1    Hicke, L.2    Palecek, J.3    Lombardi, R.4    Aust, T.5
  • 213
    • 0032917783 scopus 로고    scopus 로고
    • Disruption of a dynamin homologue affects endocytosis, organelle morphology, and cytokinesis in Dictyostelium discoideum
    • Wienke DC, Knetsch ML, Neuhaus EM, Reedy MC, Manstein DJ. 1999. Disruption of a dynamin homologue affects endocytosis, organelle morphology, and cytokinesis in Dictyostelium discoideum. Mol. Biol. Cell 10:225-43
    • (1999) Mol. Biol. Cell , vol.10 , pp. 225-243
    • Wienke, D.C.1    Knetsch, M.L.2    Neuhaus, E.M.3    Reedy, M.C.4    Manstein, D.J.5
  • 214
    • 0033528995 scopus 로고    scopus 로고
    • Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein
    • Winter D, Lechler T, Li R. 1999. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr. Biol. 9:501-4
    • (1999) Curr. Biol. , vol.9 , pp. 501-504
    • Winter, D.1    Lechler, T.2    Li, R.3
  • 215
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke W, Podtelejnikov AV, Di Nardo A, Sutherland JD, Gurniak CB, et al. 1998. In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. EMBO J. 17:967-76
    • (1998) EMBO J. , vol.17 , pp. 967-976
    • Witke, W.1    Podtelejnikov, A.V.2    Di Nardo, A.3    Sutherland, J.D.4    Gurniak, C.B.5
  • 216
    • 0021337903 scopus 로고
    • Intracellular segregation of asialoglycoproteins and their receptor: A prelysosomal event subsequent to dissociation of the ligand-receptor complex
    • Wolkoff AW, Klausner RD, Ashwell G, Harford J. 1984. Intracellular segregation of asialoglycoproteins and their receptor: a prelysosomal event subsequent to dissociation of the ligand-receptor complex. J. Cell Biol. 98: 375-81
    • (1984) J. Cell Biol. , vol.98 , pp. 375-381
    • Wolkoff, A.W.1    Klausner, R.D.2    Ashwell, G.3    Harford, J.4
  • 217
    • 0027419589 scopus 로고
    • Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu H, Parsons JT. 1993. Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120:1417-26
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 218
    • 0025940103 scopus 로고
    • Identification and characterization of a novel cytoskeleton-associated pp60src substrate
    • Wu H, Reynolds AB, Kanner SB, Vines RR, Parsons JT. 1991. Identification and characterization of a novel cytoskeleton-associated pp60src substrate. Mol. Cell. Biol. 11:5113-24
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5113-5124
    • Wu, H.1    Reynolds, A.B.2    Kanner, S.B.3    Vines, R.R.4    Parsons, J.T.5
  • 219
    • 0032553443 scopus 로고    scopus 로고
    • Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains
    • Yamabhai M, Hoffman NG, Hardison NL, McPherson PS, Castagnoli L, et al. 1998. Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains. J. Biol. Chem. 273:31401-7
    • (1998) J. Biol. Chem. , vol.273 , pp. 31401-31407
    • Yamabhai, M.1    Hoffman, N.G.2    Hardison, N.L.3    McPherson, P.S.4    Castagnoli, L.5
  • 220
    • 0032589216 scopus 로고    scopus 로고
    • Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals
    • Yang S, Cope MJ, Drubin DG. 1999. Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10:2265-83
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2265-2283
    • Yang, S.1    Cope, M.J.2    Drubin, D.G.3
  • 221
    • 0035941308 scopus 로고    scopus 로고
    • The nonreceptor tyrosine kinase ACK2, a specific target for Cdc42 and a negative regulator of cell growth and focal adhesion complexes
    • Yang W, Lin Q, Zhao J, Guan JL, Cerione RA. 2001a. The nonreceptor tyrosine kinase ACK2, a specific target for Cdc42 and a negative regulator of cell growth and focal adhesion complexes. J. Biol. Chem. 276:43987-93
    • (2001) J. Biol. Chem. , vol.276 , pp. 43987-43993
    • Yang, W.1    Lin, Q.2    Zhao, J.3    Guan, J.L.4    Cerione, R.A.5
  • 222
    • 0035907377 scopus 로고    scopus 로고
    • The Cdc42 target ACK2 directly interacts with clathrin and influences clathrin assembly
    • Yang W, Lo CG, Dispenza T, Cerione RA. 2001b. The Cdc42 target ACK2 directly interacts with clathrin and influences clathrin assembly. J. Biol. Chem. 276:17468-73
    • (2001) J. Biol. Chem. , vol.276 , pp. 17468-17473
    • Yang, W.1    Lo, C.G.2    Dispenza, T.3    Cerione, R.A.4
  • 223
    • 0032744490 scopus 로고    scopus 로고
    • Adaptor complex-independent clathrin function in yeast
    • Yeung BG, Phan HL, Payne GS. 1999. Adaptor complex-independent clathrin function in yeast. Mol. Biol. Cell 10:3643-59
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3643-3659
    • Yeung, B.G.1    Phan, H.L.2    Payne, G.S.3
  • 224
    • 0033545185 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p
    • Zeng G, Cai M. 1999. Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. J. Cell Biol. 144:71-82
    • (1999) J. Cell Biol. , vol.144 , pp. 71-82
    • Zeng, G.1    Cai, M.2
  • 225
    • 0035658368 scopus 로고    scopus 로고
    • Regulation of yeast actin cytoskeleton-regulatory complex Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p
    • Zeng G, Yu X, Cai M. 2001. Regulation of yeast actin cytoskeleton- regulatory complex Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p. Mol. Biol. Cell 12:3759-72
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3759-3772
    • Zeng, G.1    Yu, X.2    Cai, M.3
  • 226
    • 0033230229 scopus 로고    scopus 로고
    • Antigen receptor-induced activation and cytoskeletal rearrangement are impaired in Wiskott-Aldrich syndrome protein-deficient lymphocytes
    • Zhang J, Shehabeldin A, da Cruz LA, Butler J, Somani AK, et al. 1999. Antigen receptor-induced activation and cytoskeletal rearrangement are impaired in Wiskott-Aldrich syndrome protein-deficient lymphocytes. J. Exp. Med. 190:1329-42
    • (1999) J. Exp. Med. , vol.190 , pp. 1329-1342
    • Zhang, J.1    Shehabeldin, A.2    Da Cruz, L.A.3    Butler, J.4    Somani, A.K.5
  • 227
    • 1842374437 scopus 로고    scopus 로고
    • MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/ cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5
    • Zoladek T, Tobiasz A, Vaduva G, Boguta M, Martin NC, Hopper AK. 1997. MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5. Genetics 145:595-603
    • (1997) Genetics , vol.145 , pp. 595-603
    • Zoladek, T.1    Tobiasz, A.2    Vaduva, G.3    Boguta, M.4    Martin, N.C.5    Hopper, A.K.6


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