메뉴 건너뛰기




Volumn 14, Issue 2, 2003, Pages 625-641

EpsinR: An ENTH domain-containing protein that interacts with AP-1

Author keywords

[No Author keywords available]

Indexed keywords

ARF PROTEIN; BREFELDIN A; CATHEPSIN D; CLATHRIN; EPSIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); LYSOSOME ENZYME; PHOSPHATIDYLINOSITIDE; PROTEIN; PROTEIN GAP1; PROTEIN SNX9; RNA; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG;

EID: 0037328750     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-09-0552     Document Type: Article
Times cited : (182)

References (36)
  • 1
    • 0034052305 scopus 로고    scopus 로고
    • The function of the Drosophila fat facets deubiquitinating enzyme in limiting photoreceptor cell number is intimately associated with endocytosis
    • Cadavid, A.L., Ginzel, A., and Fischer, J.A. (2000). The function of the Drosophila fat facets deubiquitinating enzyme in limiting photoreceptor cell number is intimately associated with endocytosis. Development 127, 1727-1736.
    • (2000) Development , vol.127 , pp. 1727-1736
    • Cadavid, A.L.1    Ginzel, A.2    Fischer, J.A.3
  • 3
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic APZ complex
    • Collins, B.M., McCoy, A.J., Kent, H.M., Evans, P.R., and Owen, D.J. Molecular architecture and functional model of the endocytic APZ complex. Cell 109, 523-535.
    • Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 4
    • 0029416828 scopus 로고
    • The ARF1 GTPase-activating protein: Zinc finger motif and Golgi complex localization
    • Cukierman, E., Huber, I., Rotman, M., and Cassel, D. (1995). The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science 270, 1999-2002.
    • (1995) Science , vol.270 , pp. 1999-2002
    • Cukierman, E.1    Huber, I.2    Rotman, M.3    Cassel, D.4
  • 5
    • 0029123267 scopus 로고
    • Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes
    • Davidson, H.W. (1995). Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes. J. Cell Biol. 130, 797-805.
    • (1995) J. Cell Biol. , vol.130 , pp. 797-805
    • Davidson, H.W.1
  • 6
    • 0035152740 scopus 로고    scopus 로고
    • γ subunit of the AP-1 adaptor complex binds clathrin: Implications for cooperative binding in coated vesicle assembly
    • Doray, B., and Kornfeld, S. (2001). γ subunit of the AP-1 adaptor complex binds clathrin: implications for cooperative binding in coated vesicle assembly. Mol. Biol. Cell 12, 1925-1935.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1925-1935
    • Doray, B.1    Kornfeld, S.2
  • 7
    • 0033598129 scopus 로고    scopus 로고
    • Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits
    • Gaidarov, I., and Keen, J.H. (1999). Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits. J. Cell Biol. 146, 755-764.
    • (1999) J. Cell Biol. , vol.146 , pp. 755-764
    • Gaidarov, I.1    Keen, J.H.2
  • 10
    • 0034599537 scopus 로고    scopus 로고
    • A family of proteins with γ-adaptin and VHS domains that facilitate trafficking between the TGN and the vacuole/lysosome
    • Hirst, J., Lui, W.W.Y., Bright, N.A., Totty, N., Seaman, M.N.J., and Robinson, M.S. (2000). A family of proteins with γ-adaptin and VHS domains that facilitate trafficking between the TGN and the vacuole/lysosome. J. Cell Biol. 149, 67-79.
    • (2000) J. Cell Biol. , vol.149 , pp. 67-79
    • Hirst, J.1    Lui, W.W.Y.2    Bright, N.A.3    Totty, N.4    Seaman, M.N.J.5    Robinson, M.S.6
  • 11
    • 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. (1999). Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. J. Biol. Chem. 274, 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
  • 12
    • 0035021147 scopus 로고    scopus 로고
    • Trafficking of yellow-fluorescent-protein-tagged μ1 subunit of clathrin adaptor AP-1 complex in living cells
    • Huang, F., Nesterov, A., Carter, R.E., and Sorkin, A. (2001). Trafficking of yellow-fluorescent-protein-tagged μ1 subunit of clathrin adaptor AP-1 complex in living cells. Traffic 2, 345-357.
    • (2001) Traffic , vol.2 , pp. 345-357
    • Huang, F.1    Nesterov, A.2    Carter, R.E.3    Sorkin, A.4
  • 13
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis
    • Itoh, T., Koshiba, S., Kikuchi, A., Yokoyama, S., and Takenawa, T. (2001). Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 291, 1047-1051.
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1    Koshiba, S.2    Kikuchi, A.3    Yokoyama, S.4    Takenawa, T.5
  • 14
    • 0031298696 scopus 로고    scopus 로고
    • Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching
    • Jensen, O.N., Podtelejnikov, A.V., and Mann, M. (1997). Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. Anal. Chem. 69, 4741-4750.
    • (1997) Anal. Chem. , vol.69 , pp. 4741-4750
    • Jensen, O.N.1    Podtelejnikov, A.V.2    Mann, M.3
  • 15
    • 0037041026 scopus 로고    scopus 로고
    • Unusual structural organization of the endocytic proteins AP180 and epsin 1
    • Kalthoff, C., Alves, J., Urbanke, C., Knorr, R., and Ungewickell, E.J. (2002). Unusual structural organization of the endocytic proteins AP180 and epsin 1. J. Biol. Chem. 277, 8209-8216.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8209-8216
    • Kalthoff, C.1    Alves, J.2    Urbanke, C.3    Knorr, R.4    Ungewickell, E.J.5
  • 16
    • 0036049039 scopus 로고    scopus 로고
    • γ-adaptin appendage domain: Structure and binding site for Eps15 and γ-synergin
    • Kent, H.M., McMahon, H.T., Evans, P.R., Benmerah, A., and Owen, D.J. (2002). γ-Adaptin appendage domain: structure and binding site for Eps15 and γ-synergin. Structure 10, 1139-1148.
    • (2002) Structure , vol.10 , pp. 1139-1148
    • Kent, H.M.1    McMahon, H.T.2    Evans, P.R.3    Benmerah, A.4    Owen, D.J.5
  • 18
    • 0035691925 scopus 로고    scopus 로고
    • μ1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate
    • Meyer, C., Eskelinen, E.L., Guruprasad, M.R., von Figura, K., and Schu, P. (2001). μ1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate. J. Cell Sci. 114, 4469-4476.
    • (2001) J. Cell Sci. , vol.114 , pp. 4469-4476
    • Meyer, C.1    Eskelinen, E.L.2    Guruprasad, M.R.3    Von Figura, K.4    Schu, P.5
  • 19
    • 0034657033 scopus 로고    scopus 로고
    • μ1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phsophate receptors
    • Meyer, C., Zizioli, D., Lausmann, S., Eskelinen, E.L., Hamann, J., Saftig, P., von Figura, K., and Schu, P. (2000). μ1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phsophate receptors. EMBO J. 19, 2193-2203.
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.L.4    Hamann, J.5    Saftig, P.6    Von Figura, K.7    Schu, P.8
  • 20
    • 18444362426 scopus 로고    scopus 로고
    • Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain
    • Noji, T., et al. (2002). Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain. Nat. Struct. Biol. 9, 527-531.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 527-531
    • Noji, T.1
  • 21
    • 0034663990 scopus 로고    scopus 로고
    • The structure and function of the β2-adaptin appendage domain
    • Owen, D.J., Vallis, Y., Pearse, B.M., McMahon, H.T., and Evans, P.R. (2000). The structure and function of the β2-adaptin appendage domain. EMBO J. 19, 4216-4227.
    • (2000) EMBO J. , vol.19 , pp. 4216-4227
    • Owen, D.J.1    Vallis, Y.2    Pearse, B.M.3    McMahon, H.T.4    Evans, P.R.5
  • 22
    • 0033000498 scopus 로고    scopus 로고
    • A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain
    • Owen, D.J., Vallis, Y., Noble, M.E., Hunter, J.B., Daftora, T.R., Evans, P.R, and McMahon, H.T. (1999). A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain. Cell 97, 805-815.
    • (1999) Cell , vol.97 , pp. 805-815
    • Owen, D.J.1    Vallis, Y.2    Noble, M.E.3    Hunter, J.B.4    Daftora, T.R.5    Evans, P.R.6    McMahon, H.T.7
  • 23
    • 0032845769 scopus 로고    scopus 로고
    • γ-synergin: An EH domain-containing protein that interacts with γ-adaptin
    • Page, L.J., Sowerby, P.J., Lui, W.W.Y., and Robinson, M.S. (1999). γ-Synergin: an EH domain-containing protein that interacts with γ-adaptin. J. Cell Biol. 146, 993-1004.
    • (1999) J. Cell Biol. , vol.146 , pp. 993-1004
    • Page, L.J.1    Sowerby, P.J.2    Lui, W.W.Y.3    Robinson, M.S.4
  • 24
    • 0037187943 scopus 로고    scopus 로고
    • Cell biology: The ubiquitin connection
    • Riezman, H. (2002). Cell biology: the ubiquitin connection. Nature 416, 451-455.
    • (2002) Nature , vol.416 , pp. 451-455
    • Riezman, H.1
  • 25
    • 0027490848 scopus 로고
    • Assembly and targeting of adaptin chimeras in transfected cells
    • Robinson, M.S. (1993). Assembly and targeting of adaptin chimeras in transfected cells. J. Cell Biol. 123, 67-77.
    • (1993) J. Cell Biol. , vol.123 , pp. 67-77
    • Robinson, M.S.1
  • 27
    • 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. (1999). 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, 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
  • 29
    • 0027371110 scopus 로고
    • Targeting and mistargeting of plasma membrane adaptors in vitro
    • Seaman, M.N.J., Ball, C.L., and Robinson, M.S. (1993). Targeting and mistargeting of plasma membrane adaptors in vitro. J. Cell Biol. 123, 1093-1105.
    • (1993) J. Cell Biol. , vol.123 , pp. 1093-1105
    • Seaman, M.N.J.1    Ball, C.L.2    Robinson, M.S.3
  • 30
    • 0034573212 scopus 로고    scopus 로고
    • Accessory factors in clathrin-dependent synaptic vesicle endocytosis
    • Slepnev, V.I., and De Camilli, P. (2000). Accessory factors in clathrin-dependent synaptic vesicle endocytosis. Nat. Rev. Neurosci. 1, 161-172.
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 161-172
    • Slepnev, V.I.1    De Camilli, P.2
  • 31
    • 0035800730 scopus 로고    scopus 로고
    • Epsin 3 is a novel extracellular matrix-induced transcript specific to wounded epithelia
    • Spradling, K.D., McDaniel, A.E., Lohi, J., and Pilcher, B.K. (2001). Epsin 3 is a novel extracellular matrix-induced transcript specific to wounded epithelia. J. Biol. Chem. 276, 29257-29267.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29257-29267
    • Spradling, K.D.1    McDaniel, A.E.2    Lohi, J.3    Pilcher, B.K.4
  • 32
    • 0035071569 scopus 로고    scopus 로고
    • Illuminating the secretory pathway: When do we need vesicles?
    • Stephens, D.J., and Pepperkok, R. (2001). Illuminating the secretory pathway: when do we need vesicles? J. Cell Sci. 114, 1053-1059.
    • (2001) J. Cell Sci. , vol.114 , pp. 1053-1059
    • Stephens, D.J.1    Pepperkok, R.2
  • 33
    • 0036199384 scopus 로고    scopus 로고
    • The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins
    • Valdivia, R.H., Baggott, D., Chuang, J.S., and Schekman, R.W. (2002). The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins. Dev. Cell 2, 283-294.
    • (2002) Dev. Cell , vol.2 , pp. 283-294
    • Valdivia, R.H.1    Baggott, D.2    Chuang, J.S.3    Schekman, R.W.4
  • 34
    • 0037009046 scopus 로고    scopus 로고
    • Enthoprotin: A novel clathrin-associated protein identified through subcellular proteomics
    • Wasiak, S. et al. (2002). Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics. J. Cell Biol. 158, 855-862.
    • (2002) J. Cell Biol. , vol.158 , pp. 855-862
    • Wasiak, S.1
  • 35
    • 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. (1999). Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin, and are required for endocytosis. EMBO J. 18, 4383-4393.
    • (1999) EMBO J. , vol.18 , pp. 4383-4393
    • Wendland, B.1    Steece, K.E.2    Emr, S.D.3
  • 36
    • 0030881255 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment
    • West, M.A., Bright, N.A., and Robinson, M.S. (1997). The role of ADP-ribosylation factor and phospholipase D in adaptor recruitment. J. Cell Biol. 138, 1239-1254.
    • (1997) J. Cell Biol. , vol.138 , pp. 1239-1254
    • West, M.A.1    Bright, N.A.2    Robinson, M.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.