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Volumn 1761, Issue 8, 2006, Pages 897-912

BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature

Author keywords

Actin; Clathrin; Dynamin; EFC domain; Endocytosis; FCH domain; IMD domain; N WASP; PCH family; Tubulation

Indexed keywords

ACTIN; ADAPTOR PROTEIN; AMPHIPHYSIN; CLATHRIN; DYNAMIN; ENDOPHILIN; EPSIN; GUANOSINE TRIPHOSPHATASE; LIPOSOME; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PHOSPHATIDYLINOSITIDE; PROTEIN SH3; SYNAPTOJANIN; TRANSCRIPTION FACTOR AP 2;

EID: 33748288113     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.06.015     Document Type: Review
Times cited : (322)

References (181)
  • 1
  • 2
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz G.K., Prinz W.A., Shibata Y., Rist J.M., and Rapoport T.A. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124 (2006) 573-586
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 3
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 4
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman R., and Orci L. Coat proteins and vesicle budding. Science 271 (1996) 1526-1533
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 5
    • 0032878703 scopus 로고    scopus 로고
    • Clathrin: anatomy of a coat protein
    • Smith C.J., and Pearse B.M. Clathrin: anatomy of a coat protein. Trends Cell Biol. 9 (1999) 335-338
    • (1999) Trends Cell Biol. , vol.9 , pp. 335-338
    • Smith, C.J.1    Pearse, B.M.2
  • 6
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman J.E., and Orci L. Molecular dissection of the secretory pathway. Nature 355 (1992) 409-415
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 7
    • 0027467275 scopus 로고
    • Budding from Golgi membranes requires the coatomer complex of non-clathrin coat proteins
    • Orci L., Palmer D.J., Ravazzola M., Perrelet A., Amherdt M., and Rothman J.E. Budding from Golgi membranes requires the coatomer complex of non-clathrin coat proteins. Nature 362 (1993) 648-652
    • (1993) Nature , vol.362 , pp. 648-652
    • Orci, L.1    Palmer, D.J.2    Ravazzola, M.3    Perrelet, A.4    Amherdt, M.5    Rothman, J.E.6
  • 8
    • 0032503947 scopus 로고    scopus 로고
    • Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes
    • Takei K., Haucke V., Slepnev V., Farsad K., Salazar M., Chen H., and De Camilli P. Generation of coated intermediates of clathrin-mediated endocytosis on protein-free liposomes. Cell 94 (1998) 131-141
    • (1998) Cell , vol.94 , pp. 131-141
    • Takei, K.1    Haucke, V.2    Slepnev, V.3    Farsad, K.4    Salazar, M.5    Chen, H.6    De Camilli, P.7
  • 9
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer S.M., and Hinshaw J.E. Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 93 (1998) 1021-1029
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 10
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K., Slepnev V.I., Haucke V., and De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat. Cell Biol. 1 (1999) 33-39
    • (1999) Nat. Cell Biol. , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 11
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., and De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J. Cell Biol. 155 (2001) 193-200
    • (2001) J. Cell Biol. , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De Camilli, P.6
  • 13
    • 0026639178 scopus 로고
    • Amphiphysin, a novel protein associated with synaptic vesicles
    • Lichte B., Veh R.W., Meyer H.E., and Kilimann M.W. Amphiphysin, a novel protein associated with synaptic vesicles. EMBO J. 11 (1992) 2521-2530
    • (1992) EMBO J. , vol.11 , pp. 2521-2530
    • Lichte, B.1    Veh, R.W.2    Meyer, H.E.3    Kilimann, M.W.4
  • 14
    • 0028910268 scopus 로고
    • Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin
    • Sivadon P., Bauer F., Aigle M., and Crouzet M. Actin cytoskeleton and budding pattern are altered in the yeast rvs161 mutant: the Rvs161 protein shares common domains with the brain protein amphiphysin. Mol. Gen. Genet. 246 (1995) 485-495
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 485-495
    • Sivadon, P.1    Bauer, F.2    Aigle, M.3    Crouzet, M.4
  • 15
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals
    • David C., McPherson P.S., Mundigl O., and de Camilli P. A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proc. Natl. Acad Sci. U. S. A. 93 (1996) 331-335
    • (1996) Proc. Natl. Acad Sci. U. S. A. , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    de Camilli, P.4
  • 16
    • 0029741917 scopus 로고    scopus 로고
    • BIN1 is a novel MYC-interacting protein with features of a tumour suppressor
    • Sakamuro D., Elliott K.J., Wechsler-Reya R., and Prendergast G.C. BIN1 is a novel MYC-interacting protein with features of a tumour suppressor. Nat. Genet. 14 (1996) 69-77
    • (1996) Nat. Genet. , vol.14 , pp. 69-77
    • Sakamuro, D.1    Elliott, K.J.2    Wechsler-Reya, R.3    Prendergast, G.C.4
  • 17
    • 0033538570 scopus 로고    scopus 로고
    • The N terminus of amphiphysin II mediates dimerization and plasma membrane targeting
    • Ramjaun A.R., Philie J., de Heuvel E., and McPherson P.S. The N terminus of amphiphysin II mediates dimerization and plasma membrane targeting. J. Biol. Chem. 274 (1999) 19785-19791
    • (1999) J. Biol. Chem. , vol.274 , pp. 19785-19791
    • Ramjaun, A.R.1    Philie, J.2    de Heuvel, E.3    McPherson, P.S.4
  • 19
    • 0032493929 scopus 로고    scopus 로고
    • Role of phosphorylation in regulation of the assembly of endocytic coat complexes
    • Slepnev V.I., Ochoa G.C., Butler M.H., Grabs D., and De Camilli P. Role of phosphorylation in regulation of the assembly of endocytic coat complexes. Science 281 (1998) 821-824
    • (1998) Science , vol.281 , pp. 821-824
    • Slepnev, V.I.1    Ochoa, G.C.2    Butler, M.H.3    Grabs, D.4    De Camilli, P.5
  • 20
    • 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., and Crouzet M. Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns. Mol. Cell. Biol. 13 (1993) 5070-5084
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5070-5084
    • Bauer, F.1    Urdaci, M.2    Aigle, M.3    Crouzet, M.4
  • 21
    • 0030697988 scopus 로고    scopus 로고
    • Functional assessment of the yeast Rvs161 and Rvs167 protein domains
    • Sivadon P., Crouzet M., and Aigle M. Functional assessment of the yeast Rvs161 and Rvs167 protein domains. FEBS Lett. 417 (1997) 21-27
    • (1997) FEBS Lett. , vol.417 , pp. 21-27
    • Sivadon, P.1    Crouzet, M.2    Aigle, M.3
  • 22
    • 0028856410 scopus 로고
    • end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae
    • Munn A.L., Stevenson B.J., Geli M.I., and Riezman H. end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 6 (1995) 1721-1742
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1721-1742
    • Munn, A.L.1    Stevenson, B.J.2    Geli, M.I.3    Riezman, H.4
  • 23
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • Kaksonen M., Toret C.P., and Drubin D.G. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 123 (2005) 305-320
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 24
    • 0030905586 scopus 로고    scopus 로고
    • Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of Ranvier in brain and around T tubules in skeletal muscle
    • Butler M.H., David C., Ochoa G.C., Freyberg Z., Daniell L., Grabs D., Cremona O., and De Camilli P. Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of Ranvier in brain and around T tubules in skeletal muscle. J. Cell Biol. 137 (1997) 1355-1367
    • (1997) J. Cell Biol. , vol.137 , pp. 1355-1367
    • Butler, M.H.1    David, C.2    Ochoa, G.C.3    Freyberg, Z.4    Daniell, L.5    Grabs, D.6    Cremona, O.7    De Camilli, P.8
  • 26
    • 0030908644 scopus 로고    scopus 로고
    • Identification and characterization of a nerve terminal-enriched amphiphysin isoform
    • Ramjaun A.R., Micheva K.D., Bouchelet I., and McPherson P.S. Identification and characterization of a nerve terminal-enriched amphiphysin isoform. J. Biol. Chem. 272 (1997) 16700-16706
    • (1997) J. Biol. Chem. , vol.272 , pp. 16700-16706
    • Ramjaun, A.R.1    Micheva, K.D.2    Bouchelet, I.3    McPherson, P.S.4
  • 31
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takei K., McPherson P.S., Schmid S.L., and De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature 374 (1995) 186-190
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 33
    • 0030792523 scopus 로고    scopus 로고
    • Clathrin interacts specifically with amphiphysin and is displaced by dynamin
    • McMahon H.T., Wigge P., and Smith C. Clathrin interacts specifically with amphiphysin and is displaced by dynamin. FEBS Lett. 413 (1997) 319-322
    • (1997) FEBS Lett. , vol.413 , pp. 319-322
    • McMahon, H.T.1    Wigge, P.2    Smith, C.3
  • 34
    • 0031746484 scopus 로고    scopus 로고
    • Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites
    • Ramjaun A.R., and McPherson P.S. Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites. J. Neurochem. 70 (1998) 2369-2376
    • (1998) J. Neurochem. , vol.70 , pp. 2369-2376
    • Ramjaun, A.R.1    McPherson, P.S.2
  • 35
    • 0034625338 scopus 로고    scopus 로고
    • Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites
    • Slepnev V.I., Ochoa G.C., Butler M.H., and De Camilli P. Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites. J. Biol. Chem. 275 (2000) 17583-17589
    • (2000) J. Biol. Chem. , vol.275 , pp. 17583-17589
    • Slepnev, V.I.1    Ochoa, G.C.2    Butler, M.H.3    De Camilli, P.4
  • 36
    • 0035890136 scopus 로고    scopus 로고
    • Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila
    • Razzaq A., Robinson I.M., McMahon H.T., Skepper J.N., Su Y., Zelhof A.C., Jackson A.P., Gay N.J., and O'Kane C.J. Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila. Genes Dev. 15 (2001) 2967-2979
    • (2001) Genes Dev. , vol.15 , pp. 2967-2979
    • Razzaq, A.1    Robinson, I.M.2    McMahon, H.T.3    Skepper, J.N.4    Su, Y.5    Zelhof, A.C.6    Jackson, A.P.7    Gay, N.J.8    O'Kane, C.J.9
  • 38
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., and DeCamilli P. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev. Cell 9 (2005) 791-804
    • (2005) Dev. Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    DeCamilli, P.6
  • 39
    • 0030856743 scopus 로고    scopus 로고
    • Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin
    • Micheva K.D., Kay B.K., and McPherson P.S. Synaptojanin forms two separate complexes in the nerve terminal. Interactions with endophilin and amphiphysin. J. Biol. Chem. 272 (1997) 27239-27245
    • (1997) J. Biol. Chem. , vol.272 , pp. 27239-27245
    • Micheva, K.D.1    Kay, B.K.2    McPherson, P.S.3
  • 40
    • 0030739938 scopus 로고    scopus 로고
    • The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
    • Ringstad N., Nemoto Y., and DeCamilli P. The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 8569-8574
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8569-8574
    • Ringstad, N.1    Nemoto, Y.2    DeCamilli, P.3
  • 41
    • 0035837426 scopus 로고    scopus 로고
    • The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways
    • Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K., Gamblin S.J., and Smerdon S.J. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature 411 (2001) 215-219
    • (2001) Nature , vol.411 , pp. 215-219
    • Tarricone, C.1    Xiao, B.2    Justin, N.3    Walker, P.A.4    Rittinger, K.5    Gamblin, S.J.6    Smerdon, S.J.7
  • 42
    • 2542480756 scopus 로고    scopus 로고
    • The stalk region of dynamin drives the constriction of dynamin tubes
    • Chen Y.J., Zhang P., Egelman E.H., and Hinshaw J.E. The stalk region of dynamin drives the constriction of dynamin tubes. Nat. Struct. Mol. Biol. 11 (2004) 574-575
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 574-575
    • Chen, Y.J.1    Zhang, P.2    Egelman, E.H.3    Hinshaw, J.E.4
  • 43
    • 22544482948 scopus 로고    scopus 로고
    • Crystal structure of the endophilin-A1 BAR domain
    • Weissenhorn W. Crystal structure of the endophilin-A1 BAR domain. J. Mol. Biol. 351 (2005) 653-661
    • (2005) J. Mol. Biol. , vol.351 , pp. 653-661
    • Weissenhorn, W.1
  • 44
  • 45
    • 2442458996 scopus 로고    scopus 로고
    • A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein
    • Yamagishi A., Masuda M., Ohki T., Onishi H., and Mochizuki N. A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. J. Biol. Chem. 279 (2004) 14929-14936
    • (2004) J. Biol. Chem. , vol.279 , pp. 14929-14936
    • Yamagishi, A.1    Masuda, M.2    Ohki, T.3    Onishi, H.4    Mochizuki, N.5
  • 46
    • 3543025954 scopus 로고    scopus 로고
    • The BAR-domain family of proteins: a case of bending and binding?
    • Habermann B. The BAR-domain family of proteins: a case of bending and binding?. EMBO Rep. 5 (2004) 250-255
    • (2004) EMBO Rep. , vol.5 , pp. 250-255
    • Habermann, B.1
  • 47
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki H., Yamaguchi H., Suetsugu S., and Takenawa T. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 408 (2000) 732-735
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 49
    • 33644862587 scopus 로고    scopus 로고
    • Characterization of the yeast amphiphysins Rvs161p and Rvs167p reveals roles for the Rvs heterodimer in vivo
    • Friesen H., Humphries C., Ho Y., Schub O., Colwill K., and Andrews B. Characterization of the yeast amphiphysins Rvs161p and Rvs167p reveals roles for the Rvs heterodimer in vivo. Mol. Biol. Cell 17 (2006) 1306-1321
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1306-1321
    • Friesen, H.1    Humphries, C.2    Ho, Y.3    Schub, O.4    Colwill, K.5    Andrews, B.6
  • 50
    • 0035798535 scopus 로고    scopus 로고
    • Differential expression of endophilin 1 and 2 dimers at central nervous system synapses
    • Ringstad N., Nemoto Y., and De Camilli P. Differential expression of endophilin 1 and 2 dimers at central nervous system synapses. J. Biol. Chem. 276 (2001) 40424-40430
    • (2001) J. Biol. Chem. , vol.276 , pp. 40424-40430
    • Ringstad, N.1    Nemoto, Y.2    De Camilli, P.3
  • 51
    • 0031555306 scopus 로고    scopus 로고
    • Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae
    • Navarro P., Durrens P., and Aigle M. Protein-protein interaction between the RVS161 and RVS167 gene products of Saccharomyces cerevisiae. Biochim. Biophys Acta 1343 (1997) 187-192
    • (1997) Biochim. Biophys Acta , vol.1343 , pp. 187-192
    • Navarro, P.1    Durrens, P.2    Aigle, M.3
  • 54
    • 0346725004 scopus 로고    scopus 로고
    • Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling
    • Randazzo P.A., and Hirsch D.S. Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling. Cell. Signal. 16 (2004) 401-413
    • (2004) Cell. Signal. , vol.16 , pp. 401-413
    • Randazzo, P.A.1    Hirsch, D.S.2
  • 57
    • 0029762883 scopus 로고    scopus 로고
    • Enhanced degradation of EGF receptors by a sorting nexin, SNX1
    • Kurten R.C., Cadena D.L., and Gill G.N. Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science 272 (1996) 1008-1010
    • (1996) Science , vol.272 , pp. 1008-1010
    • Kurten, R.C.1    Cadena, D.L.2    Gill, G.N.3
  • 58
    • 0036904274 scopus 로고    scopus 로고
    • Sorting out the cellular functions of sorting nexins
    • Worby C.A., and Dixon J.E. Sorting out the cellular functions of sorting nexins. Nat. Rev., Mol. Cell Biol. 3 (2002) 919-931
    • (2002) Nat. Rev., Mol. Cell Biol. , vol.3 , pp. 919-931
    • Worby, C.A.1    Dixon, J.E.2
  • 59
    • 4644242944 scopus 로고    scopus 로고
    • Endophilin B1 is required for the maintenance of mitochondrial morphology
    • Karbowski M., Jeong S.Y., and Youle R.J. Endophilin B1 is required for the maintenance of mitochondrial morphology. J. Cell Biol. 166 (2004) 1027-1039
    • (2004) J. Cell Biol. , vol.166 , pp. 1027-1039
    • Karbowski, M.1    Jeong, S.Y.2    Youle, R.J.3
  • 60
    • 0346756190 scopus 로고    scopus 로고
    • Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
    • Bigay J., Gounon P., Robineau S., and Antonny B. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426 (2003) 563-566
    • (2003) Nature , vol.426 , pp. 563-566
    • Bigay, J.1    Gounon, P.2    Robineau, S.3    Antonny, B.4
  • 62
    • 20544477912 scopus 로고    scopus 로고
    • Multiple activities for Arf1 at the Golgi complex
    • Donaldson J.G., Honda A., and Weigert R. Multiple activities for Arf1 at the Golgi complex. Biochim. Biophys. Acta 1744 (2005) 364-373
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 364-373
    • Donaldson, J.G.1    Honda, A.2    Weigert, R.3
  • 63
    • 0030458832 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1-regulated phospholipase D activity is localized at the plasma membrane and intracellular organelles in HL60 cells
    • Whatmore J., Morgan C.P., Cunningham E., Collison K.S., Willison K.R., and Cockcroft S. ADP-ribosylation factor 1-regulated phospholipase D activity is localized at the plasma membrane and intracellular organelles in HL60 cells. Biochem. J. 320 Pt 3 (1996) 785-794
    • (1996) Biochem. J. , vol.320 , Issue.PART 3 , pp. 785-794
    • Whatmore, J.1    Morgan, C.P.2    Cunningham, E.3    Collison, K.S.4    Willison, K.R.5    Cockcroft, S.6
  • 65
    • 0029416828 scopus 로고
    • The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization
    • Cukierman E., Huber I., Rotman M., and Cassel D. The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science 270 (1995) 1999-2002
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 66
    • 22744442219 scopus 로고    scopus 로고
    • ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif
    • Bigay J., Casella J.F., Drin G., Mesmin B., and Antonny B. ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif. EMBO J. 24 (2005) 2244-2253
    • (2005) EMBO J. , vol.24 , pp. 2244-2253
    • Bigay, J.1    Casella, J.F.2    Drin, G.3    Mesmin, B.4    Antonny, B.5
  • 67
    • 0034656215 scopus 로고    scopus 로고
    • Involvement of PCH family proteins in cytokinesis and actin distribution
    • Lippincott J., and Li R. Involvement of PCH family proteins in cytokinesis and actin distribution. Microsc. Res. Tech. 49 (2000) 168-172
    • (2000) Microsc. Res. Tech. , vol.49 , pp. 168-172
    • Lippincott, J.1    Li, R.2
  • 68
    • 0031194076 scopus 로고    scopus 로고
    • A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton
    • Aspenstrom P. A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr. Biol. 7 (1997) 479-487
    • (1997) Curr. Biol. , vol.7 , pp. 479-487
    • Aspenstrom, P.1
  • 69
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
    • Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., and Takenawa T. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J. Cell Biol. 172 (2006) 269-279
    • (2006) J. Cell Biol. , vol.172 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3    Furutani, M.4    Oikawa, T.5    Takenawa, T.6
  • 70
    • 4544251239 scopus 로고    scopus 로고
    • A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis
    • Kamioka Y., Fukuhara S., Sawa H., Nagashima K., Masuda M., Matsuda M., and Mochizuki N. A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J. Biol. Chem. 279 (2004) 40091-40099
    • (2004) J. Biol. Chem. , vol.279 , pp. 40091-40099
    • Kamioka, Y.1    Fukuhara, S.2    Sawa, H.3    Nagashima, K.4    Masuda, M.5    Matsuda, M.6    Mochizuki, N.7
  • 71
    • 3242671847 scopus 로고    scopus 로고
    • Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex
    • Ho H.Y., Rohatgi R., Lebensohn A.M., Le M., Li J., Gygi S.P., and Kirschner M.W. Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 118 (2004) 203-216
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.1    Rohatgi, R.2    Lebensohn, A.M.3    Le, M.4    Li, J.5    Gygi, S.P.6    Kirschner, M.W.7
  • 72
    • 1342312355 scopus 로고    scopus 로고
    • Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in Drosophila
    • Coyle I.P., Koh Y.H., Lee W.C., Slind J., Fergestad T., Littleton J.T., and Ganetzky B. Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in Drosophila. Neuron 41 (2004) 521-534
    • (2004) Neuron , vol.41 , pp. 521-534
    • Coyle, I.P.1    Koh, Y.H.2    Lee, W.C.3    Slind, J.4    Fergestad, T.5    Littleton, J.T.6    Ganetzky, B.7
  • 73
    • 0030770817 scopus 로고    scopus 로고
    • FAP52, a novel, SH3 domain-containing focal adhesion protein
    • Merilainen J., Lehto V.P., and Wasenius V.M. FAP52, a novel, SH3 domain-containing focal adhesion protein. J. Biol. Chem. 272 (1997) 23278-23284
    • (1997) J. Biol. Chem. , vol.272 , pp. 23278-23284
    • Merilainen, J.1    Lehto, V.P.2    Wasenius, V.M.3
  • 74
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • Qualmann B., Roos J., DiGregorio P.J., and Kelly R.B. Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol. Biol. Cell 10 (1999) 501-513
    • (1999) Mol. Biol. Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 75
    • 0034611006 scopus 로고    scopus 로고
    • Syndapin isoforms participate in receptor-mediated endocytosis and actin organization
    • Qualmann B., and Kelly R.B. Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J. Cell Biol. 148 (2000) 1047-1062
    • (2000) J. Cell Biol. , vol.148 , pp. 1047-1062
    • Qualmann, B.1    Kelly, R.B.2
  • 76
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels M.M., and Qualmann B. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J. 21 (2002) 6083-6094
    • (2002) EMBO J. , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 80
    • 0030872948 scopus 로고    scopus 로고
    • PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase
    • Spencer S., Dowbenko D., Cheng J., Li W., Brush J., Utzig S., Simanis V., and Lasky L.A. PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphatase. J. Cell Biol. 138 (1997) 845-860
    • (1997) J. Cell Biol. , vol.138 , pp. 845-860
    • Spencer, S.1    Dowbenko, D.2    Cheng, J.3    Li, W.4    Brush, J.5    Utzig, S.6    Simanis, V.7    Lasky, L.A.8
  • 81
    • 0032489515 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein
    • Wu Y., Spencer S.D., and Lasky L.A. Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein. J. Biol. Chem. 273 (1998) 5765-5770
    • (1998) J. Biol. Chem. , vol.273 , pp. 5765-5770
    • Wu, Y.1    Spencer, S.D.2    Lasky, L.A.3
  • 83
    • 4344618740 scopus 로고    scopus 로고
    • Continuous association of cadherin with beta-catenin requires the non-receptor tyrosine-kinase Fer
    • Xu G., Craig A.W., Greer P., Miller M., Anastasiadis P.Z., Lilien J., and Balsamo J. Continuous association of cadherin with beta-catenin requires the non-receptor tyrosine-kinase Fer. J. Cell Sci. 117 (2004) 3207-3219
    • (2004) J. Cell Sci. , vol.117 , pp. 3207-3219
    • Xu, G.1    Craig, A.W.2    Greer, P.3    Miller, M.4    Anastasiadis, P.Z.5    Lilien, J.6    Balsamo, J.7
  • 84
    • 0032576546 scopus 로고    scopus 로고
    • Dual function of Cyk2, a cdc15/PSTPIP family protein, in regulating actomyosin ring dynamics and septin distribution
    • Lippincott J., and Li R. Dual function of Cyk2, a cdc15/PSTPIP family protein, in regulating actomyosin ring dynamics and septin distribution. J. Cell Biol. 143 (1998) 1947-1960
    • (1998) J. Cell Biol. , vol.143 , pp. 1947-1960
    • Lippincott, J.1    Li, R.2
  • 85
    • 0036840975 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro
    • Soulard A., Lechler T., Spiridonov V., Shevchenko A., Li R., and Winsor B. Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol. Cell. Biol. 22 (2002) 7889-7906
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7889-7906
    • Soulard, A.1    Lechler, T.2    Spiridonov, V.3    Shevchenko, A.4    Li, R.5    Winsor, B.6
  • 87
    • 0035812886 scopus 로고    scopus 로고
    • Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae
    • Roumanie O., Weinachter C., Larrieu I., Crouzet M., and Doignon F. Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae. FEBS Lett. 506 (2001) 149-156
    • (2001) FEBS Lett. , vol.506 , pp. 149-156
    • Roumanie, O.1    Weinachter, C.2    Larrieu, I.3    Crouzet, M.4    Doignon, F.5
  • 88
    • 0029112482 scopus 로고
    • The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis
    • Fankhauser C., Reymond A., Cerutti L., Utzig S., Hofmann K., and Simanis V. The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis. Cell 82 (1995) 435-444
    • (1995) Cell , vol.82 , pp. 435-444
    • Fankhauser, C.1    Reymond, A.2    Cerutti, L.3    Utzig, S.4    Hofmann, K.5    Simanis, V.6
  • 89
    • 0032547838 scopus 로고    scopus 로고
    • imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe
    • Demeter J., and Sazer S. imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe. J. Cell Biol. 143 (1998) 415-427
    • (1998) J. Cell Biol. , vol.143 , pp. 415-427
    • Demeter, J.1    Sazer, S.2
  • 90
    • 1542571932 scopus 로고    scopus 로고
    • The novel Rho GTPase-activating protein family protein, Rga8, provides a potential link between Cdc42/p21-activated kinase and Rho signaling pathways in the fission yeast, Schizosaccharomyces pombe
    • Yang P., Qyang Y., Bartholomeusz G., Zhou X., and Marcus S. The novel Rho GTPase-activating protein family protein, Rga8, provides a potential link between Cdc42/p21-activated kinase and Rho signaling pathways in the fission yeast, Schizosaccharomyces pombe. J. Biol. Chem. 278 (2003) 48821-48830
    • (2003) J. Biol. Chem. , vol.278 , pp. 48821-48830
    • Yang, P.1    Qyang, Y.2    Bartholomeusz, G.3    Zhou, X.4    Marcus, S.5
  • 93
    • 33745513790 scopus 로고    scopus 로고
    • Identification of Endophilins 1 and 3 as Selective Binding Partners for VGLUT1 and Their Co-Localization in Neocortical Glutamatergic Synapses: Implications for Vesicular Glutamate Transporter Trafficking and Excitatory Vesicle Formation
    • (in press)
    • DeGois S., Jeanclos E., Morris M., Grewal S., Varoqui H., and Erickson J.D. Identification of Endophilins 1 and 3 as Selective Binding Partners for VGLUT1 and Their Co-Localization in Neocortical Glutamatergic Synapses: Implications for Vesicular Glutamate Transporter Trafficking and Excitatory Vesicle Formation. Cell. Mol. Neurobiol. (2006) (in press)
    • (2006) Cell. Mol. Neurobiol.
    • DeGois, S.1    Jeanclos, E.2    Morris, M.3    Grewal, S.4    Varoqui, H.5    Erickson, J.D.6
  • 95
    • 0033615602 scopus 로고    scopus 로고
    • Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1
    • Howard L., Nelson K.K., Maciewicz R.A., and Blobel C.P. Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. J. Biol. Chem. 274 (1999) 31693-31699
    • (1999) J. Biol. Chem. , vol.274 , pp. 31693-31699
    • Howard, L.1    Nelson, K.K.2    Maciewicz, R.A.3    Blobel, C.P.4
  • 98
  • 99
    • 33748315186 scopus 로고    scopus 로고
    • G. Di Paolo, P. De Camilli, Phosphoinositides in Cell Regulation and Membrane Dynamics, Nature (in press).
  • 100
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia R., and Munro S. Organelle identity and the signposts for membrane traffic. Nature 438 (2005) 597-604
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 101
    • 0031041589 scopus 로고    scopus 로고
    • Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes
    • Kanoh H., Williger B.T., and Exton J.H. Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. J. Biol. Chem. 272 (1997) 5421-5429
    • (1997) J. Biol. Chem. , vol.272 , pp. 5421-5429
    • Kanoh, H.1    Williger, B.T.2    Exton, J.H.3
  • 102
    • 0029757748 scopus 로고    scopus 로고
    • Identification of a novel Rac1-interacting protein involved in membrane ruffling
    • Van Aelst L., Joneson T., and Bar-Sagi D. Identification of a novel Rac1-interacting protein involved in membrane ruffling. EMBO J. 15 (1996) 3778-3786
    • (1996) EMBO J. , vol.15 , pp. 3778-3786
    • Van Aelst, L.1    Joneson, T.2    Bar-Sagi, D.3
  • 105
    • 0033575748 scopus 로고    scopus 로고
    • Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis
    • Wendland B., Steece K.E., and Emr S.D. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 18 (1999) 4383-4393
    • (1999) EMBO J. , vol.18 , pp. 4383-4393
    • Wendland, B.1    Steece, K.E.2    Emr, S.D.3
  • 106
    • 0033005568 scopus 로고    scopus 로고
    • Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery
    • Kay B.K., Yamabhai M., Wendl B., and Emr S.D. Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery. Protein Sci. 8 (1999) 435-438
    • (1999) Protein Sci. , vol.8 , pp. 435-438
    • Kay, B.K.1    Yamabhai, M.2    Wendl, B.3    Emr, S.D.4
  • 107
    • 0036902815 scopus 로고    scopus 로고
    • Epsins: adaptors in endocytosis?
    • Wendland B. Epsins: adaptors in endocytosis?. Nat. Rev., Mol. Cell Biol. 3 (2002) 971-977
    • (2002) Nat. Rev., Mol. Cell Biol. , vol.3 , pp. 971-977
    • Wendland, B.1
  • 108
    • 0033607806 scopus 로고    scopus 로고
    • The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module
    • Rosenthal J.A., Chen H., Slepnev V.I., Pellegrini L., Salcini A.E., Di Fiore P.P., and De Camilli P. The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module. J. Biol. Chem. 274 (1999) 33959-33965
    • (1999) J. Biol. Chem. , vol.274 , pp. 33959-33965
    • Rosenthal, J.A.1    Chen, H.2    Slepnev, V.I.3    Pellegrini, L.4    Salcini, A.E.5    Di Fiore, P.P.6    De Camilli, P.7
  • 109
    • 0034010261 scopus 로고    scopus 로고
    • Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites
    • Drake M.T., Downs M.A., and Traub L.M. Epsin binds to clathrin by associating directly with the clathrin-terminal domain. Evidence for cooperative binding through two discrete sites. J. Biol. Chem. 275 (2000) 6479-6489
    • (2000) J. Biol. Chem. , vol.275 , pp. 6479-6489
    • Drake, M.T.1    Downs, M.A.2    Traub, L.M.3
  • 113
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih S.C., Katzmann D.J., Schnell J.D., Sutanto M., Emr S.D., and Hicke L. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4 (2002) 389-393
    • (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
  • 114
    • 14544288669 scopus 로고    scopus 로고
    • The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin
    • Chen H., and De Camilli P. The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin. Proc. Natl. Acad Sci. U. S. A. 102 (2005) 2766-2771
    • (2005) Proc. Natl. Acad Sci. U. S. A. , vol.102 , pp. 2766-2771
    • Chen, H.1    De Camilli, P.2
  • 116
    • 0037518120 scopus 로고    scopus 로고
    • The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions
    • Aguilar R.C., Watson H.A., and Wendland B. The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions. J. Biol. Chem. 278 (2003) 10737-10743
    • (2003) J. Biol. Chem. , vol.278 , pp. 10737-10743
    • Aguilar, R.C.1    Watson, H.A.2    Wendland, B.3
  • 118
    • 9444297354 scopus 로고    scopus 로고
    • Drosophila Epsin mediates a select endocytic pathway that DSL ligands must enter to activate Notch
    • Wang W., and Struhl G. Drosophila Epsin mediates a select endocytic pathway that DSL ligands must enter to activate Notch. Development 131 (2004) 5367-5380
    • (2004) Development , vol.131 , pp. 5367-5380
    • Wang, W.1    Struhl, G.2
  • 119
    • 9544221645 scopus 로고    scopus 로고
    • Fat facets and Liquid facets promote Delta endocytosis and Delta signaling in the signaling cells
    • Overstreet E., Fitch E., and Fischer J.A. Fat facets and Liquid facets promote Delta endocytosis and Delta signaling in the signaling cells. Development 131 (2004) 5355-5366
    • (2004) Development , vol.131 , pp. 5355-5366
    • Overstreet, E.1    Fitch, E.2    Fischer, J.A.3
  • 120
    • 0042707772 scopus 로고    scopus 로고
    • Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains
    • Stahelin R.V., Long F., Peter B.J., Murray D., De Camilli P., McMahon H.T., and Cho W. Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. J. Biol. Chem. 278 (2003) 28993-28999
    • (2003) J. Biol. Chem. , vol.278 , pp. 28993-28999
    • Stahelin, R.V.1    Long, F.2    Peter, B.J.3    Murray, D.4    De Camilli, P.5    McMahon, H.T.6    Cho, W.7
  • 121
    • 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., and Takenawa T. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 291 (2001) 1047-1051
    • (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
  • 124
    • 0034192540 scopus 로고    scopus 로고
    • Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)
    • Hyman J., Chen H., Di Fiore P.P., De Camilli P., and Brunger A.T. Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF). J. Cell Biol. 149 (2000) 537-546
    • (2000) J. Cell Biol. , vol.149 , pp. 537-546
    • Hyman, J.1    Chen, H.2    Di Fiore, P.P.3    De Camilli, P.4    Brunger, A.T.5
  • 125
    • 0036293634 scopus 로고    scopus 로고
    • Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin
    • Koshiba S., Kigawa T., Kikuchi A., and Yokoyama S. Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin. J. Struct. Funct Genomics 2 (2002) 1-8
    • (2002) J. Struct. Funct Genomics , vol.2 , pp. 1-8
    • Koshiba, S.1    Kigawa, T.2    Kikuchi, A.3    Yokoyama, S.4
  • 132
    • 3042723253 scopus 로고    scopus 로고
    • Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body
    • Eugster A., Pecheur E.I., Michel F., Winsor B., Letourneur F., and Friant S. Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol. Biol. Cell 15 (2004) 3031-3041
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3031-3041
    • Eugster, A.1    Pecheur, E.I.2    Michel, F.3    Winsor, B.4    Letourneur, F.5    Friant, S.6
  • 133
    • 1042278166 scopus 로고    scopus 로고
    • Specific interaction between SNAREs and epsin N-terminal homology (ENTH) domains of epsin-related proteins in trans-Golgi network to endosome transport
    • Chidambaram S., Mullers N., Wiederhold K., Haucke V., and von Mollard G.F. Specific interaction between SNAREs and epsin N-terminal homology (ENTH) domains of epsin-related proteins in trans-Golgi network to endosome transport. J. Biol. Chem. 279 (2004) 4175-4179
    • (2004) J. Biol. Chem. , vol.279 , pp. 4175-4179
    • Chidambaram, S.1    Mullers, N.2    Wiederhold, K.3    Haucke, V.4    von Mollard, G.F.5
  • 137
    • 0026635028 scopus 로고
    • Characterization of a novel synapse-specific protein. II. cDNA cloning and sequence analysis of the F1-20 protein
    • Zhou S., Sousa R., Tannery N.H., and Lafer E.M. Characterization of a novel synapse-specific protein. II. cDNA cloning and sequence analysis of the F1-20 protein. J. Neurosci. 12 (1992) 2144-2155
    • (1992) J. Neurosci. , vol.12 , pp. 2144-2155
    • Zhou, S.1    Sousa, R.2    Tannery, N.H.3    Lafer, E.M.4
  • 138
    • 0026637449 scopus 로고
    • Characterization of a novel synapse-specific protein. I. Developmental expression and cellular localization of the F1-20 protein and mRNA
    • Sousa R., Tannery N.H., Zhou S., and Lafer E.M. Characterization of a novel synapse-specific protein. I. Developmental expression and cellular localization of the F1-20 protein and mRNA. J. Neurosci. 12 (1992) 2130-2143
    • (1992) J. Neurosci. , vol.12 , pp. 2130-2143
    • Sousa, R.1    Tannery, N.H.2    Zhou, S.3    Lafer, E.M.4
  • 139
    • 0025898416 scopus 로고
    • Clathrin assembly protein AP-3. The identity of the 155K protein, AP 180, and NP185 and demonstration of a clathrin binding domain
    • Murphy J.E., Pleasure I.T., Puszkin S., Prasad K., and Keen J.H. Clathrin assembly protein AP-3. The identity of the 155K protein, AP 180, and NP185 and demonstration of a clathrin binding domain. J. Biol. Chem. 266 (1991) 4401-4408
    • (1991) J. Biol. Chem. , vol.266 , pp. 4401-4408
    • Murphy, J.E.1    Pleasure, I.T.2    Puszkin, S.3    Prasad, K.4    Keen, J.H.5
  • 140
    • 0028955339 scopus 로고
    • Clathrin binding and assembly activities of expressed domains of the synapse-specific clathrin assembly protein AP-3
    • Ye W., and Lafer E.M. Clathrin binding and assembly activities of expressed domains of the synapse-specific clathrin assembly protein AP-3. J. Biol. Chem. 270 (1995) 10933-10939
    • (1995) J. Biol. Chem. , vol.270 , pp. 10933-10939
    • Ye, W.1    Lafer, E.M.2
  • 142
    • 0037014445 scopus 로고    scopus 로고
    • Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans
    • Burbea M., Dreier L., Dittman J.S., Grunwald M.E., and Kaplan J.M. Ubiquitin and AP180 regulate the abundance of GLR-1 glutamate receptors at postsynaptic elements in C. elegans. Neuron 35 (2002) 107-120
    • (2002) Neuron , vol.35 , pp. 107-120
    • Burbea, M.1    Dreier, L.2    Dittman, J.S.3    Grunwald, M.E.4    Kaplan, J.M.5
  • 143
    • 0032807691 scopus 로고    scopus 로고
    • Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic
    • Tebar F., Bohlander S.K., and Sorkin A. Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic. Mol. Biol. Cell 10 (1999) 2687-2702
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2687-2702
    • Tebar, F.1    Bohlander, S.K.2    Sorkin, A.3
  • 144
    • 0027480960 scopus 로고    scopus 로고
    • HDCRG, A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group, Cell 72 (1993) 971-83.
  • 146
    • 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 A.E., Kessels M.M., Chopra V.S., Hayden M.R., and Drubin D.G. 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 (1999) 1503-1518
    • (1999) J. Cell Biol. , vol.147 , pp. 1503-1518
    • Engqvist-Goldstein, A.E.1    Kessels, M.M.2    Chopra, V.S.3    Hayden, M.R.4    Drubin, D.G.5
  • 148
    • 0031700674 scopus 로고    scopus 로고
    • Cloning, expression analysis, and chromosomal localization of HIP1R, an isolog of huntingtin interacting protein (HIP1)
    • Seki N., Muramatsu M., Sugano S., Suzuki Y., Nakagawara A., Ohhira M., Hayashi A., Hori T., and Saito T. Cloning, expression analysis, and chromosomal localization of HIP1R, an isolog of huntingtin interacting protein (HIP1). J. Hum. Genet. 43 (1998) 268-271
    • (1998) J. Hum. Genet. , vol.43 , pp. 268-271
    • Seki, N.1    Muramatsu, M.2    Sugano, S.3    Suzuki, Y.4    Nakagawara, A.5    Ohhira, M.6    Hayashi, A.7    Hori, T.8    Saito, T.9
  • 149
    • 0032589216 scopus 로고    scopus 로고
    • Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals
    • Yang S., Cope M.J., and Drubin D.G. Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10 (1999) 2265-2283
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2265-2283
    • Yang, S.1    Cope, M.J.2    Drubin, D.G.3
  • 150
    • 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., Munn A.L., and Riezman H. End4p/Sla2p interacts with actin-associated proteins for endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell 8 (1997) 2291-2306
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2291-2306
    • Wesp, A.1    Hicke, L.2    Palecek, J.3    Lombardi, R.4    Aust, T.5    Munn, A.L.6    Riezman, H.7
  • 151
    • 1642464687 scopus 로고    scopus 로고
    • RNAi-mediated Hip1R silencing results in stable association between the endocytic machinery and the actin assembly machinery
    • Engqvist-Goldstein A.E., Zhang C.X., Carreno S., Barroso C., Heuser J.E., and Drubin D.G. RNAi-mediated Hip1R silencing results in stable association between the endocytic machinery and the actin assembly machinery. Mol. Biol. Cell 15 (2004) 1666-1679
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1666-1679
    • Engqvist-Goldstein, A.E.1    Zhang, C.X.2    Carreno, S.3    Barroso, C.4    Heuser, J.E.5    Drubin, D.G.6
  • 152
    • 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 A.E., Warren R.A., Kessels M.M., Keen J.H., Heuser J., and Drubin D.G. The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro. J. Cell Biol. 154 (2001) 1209-1223
    • (2001) J. Cell Biol. , vol.154 , pp. 1209-1223
    • Engqvist-Goldstein, A.E.1    Warren, R.A.2    Kessels, M.M.3    Keen, J.H.4    Heuser, J.5    Drubin, D.G.6
  • 153
    • 0035830502 scopus 로고    scopus 로고
    • A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis
    • Mao Y., Chen J., Maynard J.A., Zhang B., and Quiocho F.A. A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis. Cell 104 (2001) 433-440
    • (2001) Cell , vol.104 , pp. 433-440
    • Mao, Y.1    Chen, J.2    Maynard, J.A.3    Zhang, B.4    Quiocho, F.A.5
  • 155
    • 0029763997 scopus 로고    scopus 로고
    • Identification and cloning of centaurin-alpha. A novel phosphatidylinositol 3,4,5-trisphosphate-binding protein from rat brain
    • Hammonds-Odie L.P., Jackson T.R., Profit A.A., Blader I.J., Turck C.W., Prestwich G.D., and Theibert A.B. Identification and cloning of centaurin-alpha. A novel phosphatidylinositol 3,4,5-trisphosphate-binding protein from rat brain. J. Biol. Chem. 271 (1996) 18859-18868
    • (1996) J. Biol. Chem. , vol.271 , pp. 18859-18868
    • Hammonds-Odie, L.P.1    Jackson, T.R.2    Profit, A.A.3    Blader, I.J.4    Turck, C.W.5    Prestwich, G.D.6    Theibert, A.B.7
  • 157
    • 0030893931 scopus 로고    scopus 로고
    • Regulation of AP-3 function by inositides. Identification of phosphatidylinositol 3,4,5-trisphosphate as a potent ligand
    • Hao W., Tan Z., Prasad K., Reddy K.K., Chen J., Prestwich G.D., Falck J.R., Shears S.B., and Lafer E.M. Regulation of AP-3 function by inositides. Identification of phosphatidylinositol 3,4,5-trisphosphate as a potent ligand. J. Biol. Chem. 272 (1997) 6393-6398
    • (1997) J. Biol. Chem. , vol.272 , pp. 6393-6398
    • Hao, W.1    Tan, Z.2    Prasad, K.3    Reddy, K.K.4    Chen, J.5    Prestwich, G.D.6    Falck, J.R.7    Shears, S.B.8    Lafer, E.M.9
  • 158
    • 0032441527 scopus 로고    scopus 로고
    • VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking
    • Lohi O., and Lehto V.P. VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking. FEBS Lett. 440 (1998) 255-257
    • (1998) FEBS Lett. , vol.440 , pp. 255-257
    • Lohi, O.1    Lehto, V.P.2
  • 159
    • 0034599537 scopus 로고    scopus 로고
    • A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome
    • Hirst J., Lui W.W., Bright N.A., Totty N., Seaman M.N., and Robinson M.S. A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome. J. Cell Biol. 149 (2000) 67-80
    • (2000) J. Cell Biol. , vol.149 , pp. 67-80
    • Hirst, J.1    Lui, W.W.2    Bright, N.A.3    Totty, N.4    Seaman, M.N.5    Robinson, M.S.6
  • 161
    • 0033151614 scopus 로고    scopus 로고
    • Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis
    • Komada M., and Soriano P. Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis. Genes Dev. 13 (1999) 1475-1485
    • (1999) Genes Dev. , vol.13 , pp. 1475-1485
    • Komada, M.1    Soriano, P.2
  • 163
  • 164
    • 0035958856 scopus 로고    scopus 로고
    • Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains
    • Takatsu H., Katoh Y., Shiba Y., and Nakayama K. Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276 (2001) 28541-28545
    • (2001) J. Biol. Chem. , vol.276 , pp. 28541-28545
    • Takatsu, H.1    Katoh, Y.2    Shiba, Y.3    Nakayama, K.4
  • 165
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor
    • Zhu Y., Doray B., Poussu A., Lehto V.P., and Kornfeld S. Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science 292 (2001) 1716-1718
    • (2001) Science , vol.292 , pp. 1716-1718
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.P.4    Kornfeld, S.5
  • 169
    • 0043238695 scopus 로고    scopus 로고
    • The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1)
    • Davies S.M., Harroun T.A., Hauss T., Kelly S.M., and Bradshaw J.P. The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1). FEBS Lett. 548 (2003) 119-124
    • (2003) FEBS Lett. , vol.548 , pp. 119-124
    • Davies, S.M.1    Harroun, T.A.2    Hauss, T.3    Kelly, S.M.4    Bradshaw, J.P.5
  • 170
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • Lee M.C., Orci L., Hamamoto S., Futai E., Ravazzola M., and Schekman R. Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122 (2005) 605-617
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 171
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • Bielli A., Haney C.J., Gabreski G., Watkins S.C., Bannykh S.I., and Aridor M. Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J. Cell Biol. 171 (2005) 919-924
    • (2005) J. Cell Biol. , vol.171 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 172
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • Amor J.C., Harrison D.H., Kahn R.A., and Ringe D. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372 (1994) 704-708
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 173
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • Antonny B., Beraud-Dufour S., Chardin P., and Chabre M. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36 (1997) 4675-4684
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 174
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg J. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95 (1998) 237-248
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 175
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • Bi X., Corpina R.A., and Goldberg J. Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419 (2002) 271-277
    • (2002) Nature , vol.419 , pp. 271-277
    • Bi, X.1    Corpina, R.A.2    Goldberg, J.3
  • 177
    • 28444437745 scopus 로고    scopus 로고
    • Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission
    • Gallop J.L., Butler P.J., and McMahon H.T. Endophilin and CtBP/BARS are not acyl transferases in endocytosis or Golgi fission. Nature 438 (2005) 675-678
    • (2005) Nature , vol.438 , pp. 675-678
    • Gallop, J.L.1    Butler, P.J.2    McMahon, H.T.3
  • 178
    • 0034677932 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules
    • Tian L., Nelson D.L., and Stewart D.M. Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules. J. Biol. Chem. 275 (2000) 7854-7861
    • (2000) J. Biol. Chem. , vol.275 , pp. 7854-7861
    • Tian, L.1    Nelson, D.L.2    Stewart, D.M.3
  • 179
    • 6344242879 scopus 로고    scopus 로고
    • The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly
    • Laurent C.E., Delfino F.J., Cheng H.Y., and Smithgall T.E. The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly. Mol. Cell. Biol. 24 (2004) 9351-9358
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9351-9358
    • Laurent, C.E.1    Delfino, F.J.2    Cheng, H.Y.3    Smithgall, T.E.4
  • 181
    • 0037160026 scopus 로고    scopus 로고
    • Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching
    • Fujita H., Katoh H., Ishikawa Y., Mori K., and Negishi M. Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching. J. Biol. Chem. 277 (2002) 45428-45434
    • (2002) J. Biol. Chem. , vol.277 , pp. 45428-45434
    • Fujita, H.1    Katoh, H.2    Ishikawa, Y.3    Mori, K.4    Negishi, M.5


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