메뉴 건너뛰기




Volumn 57, Issue 2, 1997, Pages 240-245

Mapping of the molecular determinants involved in the interaction between eps15 and AP-2

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE; TRANSCRIPTION FACTOR AP 1;

EID: 0031032314     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (87)

References (40)
  • 2
    • 0028318695 scopus 로고
    • The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31-p32
    • Wong, W. T., Kraus, M. H., Carlomagno, F., Zelano, A., Druck, T., Croce, C. M., Huebner, K., and Di Fiore, P. P. The human eps15 gene, encoding a tyrosine kinase substrate, is conserved in evolution and maps to 1p31-p32. Oncogene, 9: 1591-1597, 1994.
    • (1994) Oncogene , vol.9 , pp. 1591-1597
    • Wong, W.T.1    Kraus, M.H.2    Carlomagno, F.3    Zelano, A.4    Druck, T.5    Croce, C.M.6    Huebner, K.7    Di Fiore, P.P.8
  • 4
    • 0029036124 scopus 로고
    • The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R
    • Schumacher, C., Knudsen, B. S., Ohuchi, T., Di Fiore, P. P., Glassman, R. H., and Hanafusa, H. The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R. J. Biol. Chem., 270: 15341-15347, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15341-15347
    • Schumacher, C.1    Knudsen, B.S.2    Ohuchi, T.3    Di Fiore, P.P.4    Glassman, R.H.5    Hanafusa, H.6
  • 6
    • 0026496887 scopus 로고
    • The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, rax, to the AF-4 gene
    • Gu, Y., Nakamura, T., Alder, H., Prasad, R., Canaani, O., Cimino, G., Croce, C. M., and Canaani, E. The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, rax, to the AF-4 gene. Cell, 71: 701-708, 1992.
    • (1992) Cell , vol.71 , pp. 701-708
    • Gu, Y.1    Nakamura, T.2    Alder, H.3    Prasad, R.4    Canaani, O.5    Cimino, G.6    Croce, C.M.7    Canaani, E.8
  • 7
    • 0026454451 scopus 로고
    • Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias
    • Tkachuk, D. C., Kohler, S., and Cleary, M. L. Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell, 71: 691-700, 1992.
    • (1992) Cell , vol.71 , pp. 691-700
    • Tkachuk, D.C.1    Kohler, S.2    Cleary, M.L.3
  • 8
    • 0028215338 scopus 로고
    • A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9, or ENL
    • Bernard, O. A., Mauchauffe, M., Mecucci, C., Van den Berghe, H., and Berger, R. A novel gene, AF-1p, fused to HRX in t(1;11)(p32;q23), is not related to AF-4, AF-9, or ENL. Oncogene, 9: 1039-1045, 1994.
    • (1994) Oncogene , vol.9 , pp. 1039-1045
    • Bernard, O.A.1    Mauchauffe, M.2    Mecucci, C.3    Van Den Berghe, H.4    Berger, R.5
  • 9
    • 0026447591 scopus 로고
    • The der(11) chromosome contains the critical breakpoint junction in the 4; 11, 9; 11, and 11:19 translocations in acute leukemia
    • Rowley, J.D. The der(11) chromosome contains the critical breakpoint junction in the 4; 11, 9; 11, and 11:19 translocations in acute leukemia. Genes Chromosomes Cancer, 5: 264-266, 1992.
    • (1992) Genes Chromosomes Cancer , vol.5 , pp. 264-266
    • Rowley, J.D.1
  • 10
    • 0029615380 scopus 로고
    • The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2
    • Benmerah, A., Gagnon, J., Begue, B., Megarbane, B., Dautry-Varsat, A., and CerfBensussan, N. The tyrosine kinase substrate eps15 is constitutively associated with the plasma membrane adaptor AP-2. J. Cell Biol., 131: 1831-1838, 1995.
    • (1995) J. Cell Biol. , vol.131 , pp. 1831-1838
    • Benmerah, A.1    Gagnon, J.2    Begue, B.3    Megarbane, B.4    Dautry-Varsat, A.5    CerfBensussan, N.6
  • 11
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson, M. S. The role of clathrin, adaptors and dynamin in endocytosis. Curr. Opin. Cell Biol., 6: 538-544, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 12
    • 0025345414 scopus 로고
    • Clathrin and associated assembly and disassembly proteins
    • Keen, J. H. Clathrin and associated assembly and disassembly proteins. Annul Rev. Biochem., 59: 415-438, 1990.
    • (1990) Annul Rev. Biochem. , vol.59 , pp. 415-438
    • Keen, J.H.1
  • 14
    • 0027249993 scopus 로고
    • Interaction of activated EGF receptors with coated pit adapting
    • Sorkin, A., and Carpenter, G. Interaction of activated EGF receptors with coated pit adapting. Science (Washington DC), 261: 612-615, 1993.
    • (1993) Science (Washington DC) , vol.261 , pp. 612-615
    • Sorkin, A.1    Carpenter, G.2
  • 15
    • 0028944988 scopus 로고
    • Stoichiometric interaction of the epidermal growth factor receptor with the clathrin-associated protein complex AP-2
    • Sorkin, A., McKinsey, T., Shih, W., Kirchhausen, T., and Carpenter, G. Stoichiometric interaction of the epidermal growth factor receptor with the clathrin-associated protein complex AP-2. J. Biol. Chem., 270: 619-625, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 619-625
    • Sorkin, A.1    McKinsey, T.2    Shih, W.3    Kirchhausen, T.4    Carpenter, G.5
  • 16
    • 0029037863 scopus 로고
    • Ligand-induced endocytosis of epidermal growth factor receptors that are defective in binding adaptor proteins
    • Nesterov, A., Wiley, H. S., and Gill, G. N. Ligand-induced endocytosis of epidermal growth factor receptors that are defective in binding adaptor proteins. Proc. Natl. Acad. Sci. USA, 92: 8719-8723, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8719-8723
    • Nesterov, A.1    Wiley, H.S.2    Gill, G.N.3
  • 17
    • 0029889579 scopus 로고    scopus 로고
    • Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif
    • Sorkin, A., Mazzotti, M., Sorkina, T., Scotto, L., and Beguinot, L. Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif. J. Biol. Chem., 271: 13377-13384, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13377-13384
    • Sorkin, A.1    Mazzotti, M.2    Sorkina, T.3    Scotto, L.4    Beguinot, L.5
  • 18
    • 0023663896 scopus 로고
    • Overexpression of the human EGF receptor confers an EGF-dependent transformed phenotype to NIH 3T3 cells
    • Di Fiore, P. P., Pierce, J. H., Fleming, T. P., Hazan, R., Ullrich, A., King, C. R., Schlessinger, J., and Aaronson, S. A. Overexpression of the human EGF receptor confers an EGF-dependent transformed phenotype to NIH 3T3 cells. Cell, 51: 1063-1070, 1987.
    • (1987) Cell , vol.51 , pp. 1063-1070
    • Di Fiore, P.P.1    Pierce, J.H.2    Fleming, T.P.3    Hazan, R.4    Ullrich, A.5    King, C.R.6    Schlessinger, J.7    Aaronson, S.A.8
  • 19
    • 0029054142 scopus 로고
    • Constitutive phosphorylation of eps8 in tumor cell lines: Relevance to malignant transformation
    • Matoskova, B., Wong, W, T., Salcini, A. E., Pelicci, P. G., and Di Fiore P. P. Constitutive phosphorylation of eps8 in tumor cell lines: relevance to malignant transformation. Mol. Cell. Biol., 15: 3805-3812, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3805-3812
    • Matoskova, B.1    Wong, W.T.2    Salcini, A.E.3    Pelicci, P.G.4    Di Fiore, P.P.5
  • 20
    • 0024523484 scopus 로고
    • Cloning of cDNAs encoding two related 100-kD-coated vesicle proteins (alpha-adaptins)
    • Robinson, M. S. Cloning of cDNAs encoding two related 100-kD-coated vesicle proteins (alpha-adaptins). J. Cell Biol., 108: 833-842, 1989.
    • (1989) J. Cell Biol. , vol.108 , pp. 833-842
    • Robinson, M.S.1
  • 21
    • 0028783372 scopus 로고
    • The alpha chain of the AP-2 adaptor is a clathrin binding subunit
    • Goodman, O. B., and Keen, J. H. The alpha chain of the AP-2 adaptor is a clathrin binding subunit. J. Biol. Chem., 270: 23768-23773, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23768-23773
    • Goodman, O.B.1    Keen, J.H.2
  • 22
    • 0023550870 scopus 로고
    • Clathrin assembly proteins: Affinity purification and a model for coat assembly
    • Keen, J. H. Clathrin assembly proteins: affinity purification and a model for coat assembly. J. Cell Biol., 105: 1989-1998, 1987.
    • (1987) J. Cell Biol. , vol.105 , pp. 1989-1998
    • Keen, J.H.1
  • 23
    • 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., 226: 4401-4408, 1991.
    • (1991) J. Biol. Chem. , vol.226 , pp. 4401-4408
    • Murphy, J.E.1    Pleasure, I.T.2    Puszkin, S.3    Prasad, K.4    Keen, J.H.5
  • 25
    • 0024075871 scopus 로고
    • Deep-etch visualization of proteins involved in clathrin assembly
    • Heuser, J. E., and Keen, J. H. Deep-etch visualization of proteins involved in clathrin assembly. J. Cell Biol., 107: 877-886, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 877-886
    • Heuser, J.E.1    Keen, J.H.2
  • 26
    • 0021792248 scopus 로고
    • Limited proteolytic digestion of coated vesicle assembly polypeptides abolishes reassembly activity
    • Zaremba, S., and Keen, J. H. Limited proteolytic digestion of coated vesicle assembly polypeptides abolishes reassembly activity. J. Cell. Biochem., 28: 47-58, 1985.
    • (1985) J. Cell. Biochem. , vol.28 , pp. 47-58
    • Zaremba, S.1    Keen, J.H.2
  • 27
    • 0024514979 scopus 로고
    • Structural and functional division into two domains of the large (100- To 115-kDa) chains of the clathrin associated protein complex AP-2
    • Kirchhausen, T., Nathanson, K. L., Matsui, W., Vaisberg, A., Chow, E. P., Burne, C., Keen, J. H., and Davis, A. E. Structural and functional division into two domains of the large (100- to 115-kDa) chains of the clathrin associated protein complex AP-2. Proc. Natl. Acad. Sci. USA, 86: 2612-2616, 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2612-2616
    • Kirchhausen, T.1    Nathanson, K.L.2    Matsui, W.3    Vaisberg, A.4    Chow, E.P.5    Burne, C.6    Keen, J.H.7    Davis, A.E.8
  • 28
    • 15844361829 scopus 로고    scopus 로고
    • The ear of α-adaptin interacts with the COOH-terminal domain of the eps15 protein
    • Benmerah, A., Bègue, B., Dautry-Varsat, A., and Cerf-Bensussan, N. The ear of α-adaptin interacts with the COOH-terminal domain of the eps15 protein. J. Biol. Chem., 271: 12111-12116, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12111-12116
    • Benmerah, A.1    Bègue, B.2    Dautry-Varsat, A.3    Cerf-Bensussan, N.4
  • 29
    • 0024317024 scopus 로고
    • Identification of a clathrin binding subunit in the HA2 adaptor protein complex
    • Ahle, S., and Ungewickell, E. Identification of a clathrin binding subunit in the HA2 adaptor protein complex. J. Biol. Chem., 264: 20089-20093, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20089-20093
    • Ahle, S.1    Ungewickell, E.2
  • 30
    • 0028986797 scopus 로고
    • The appendage domain of α-adaptin is a high affinity binding site for dynamin
    • Wang, L. H., Sudhof, T. C., and Anderson, R. G. W. The appendage domain of α-adaptin is a high affinity binding site for dynamin. J. Biol. Chem., 270: 10079-10083, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10079-10083
    • Wang, L.H.1    Sudhof, T.C.2    Anderson, R.G.W.3
  • 32
    • 0028168590 scopus 로고
    • Synaptotagmin I is a high affinity receptor for clathrin AP-2: Implications for membrane recycling
    • Zhang, J. Z., Davletov, B. Z., Sudhof, T. C., and Anderson, R. G. Synaptotagmin I is a high affinity receptor for clathrin AP-2: implications for membrane recycling. Cell, 78: 751-760, 1994.
    • (1994) Cell , vol.78 , pp. 751-760
    • Zhang, J.Z.1    Davletov, B.Z.2    Sudhof, T.C.3    Anderson, R.G.4
  • 33
    • 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. USA, 93: 331-335, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    De Camilli, P.4
  • 36
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke, H., Baba, T., Warnock, D. E., and Schmid, S. L. Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol., 127: 915-934, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 37
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw, J. E., and Schmid, S. L. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature (Lond.), 374: 190-192, 1995.
    • (1995) Nature (Lond.) , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 38
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated dynamin rings are induced by GTP gamma S in nerve terminals
    • Takel, K., McPherson, P. S., Schmid, S. L., and De Camilli, P. Tubular membrane invaginations coated dynamin rings are induced by GTP gamma S in nerve terminals. Nature (Lond.), 374: 186-190, 1995.
    • (1995) Nature (Lond.) , vol.374 , pp. 186-190
    • Takel, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 39
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleion organization in yeast
    • Benedetti, H., Raths, S., Crausaz, F., and Riezman, H. The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleion organization in yeast. Mol. Biol. Cell, 5: 1023-1037, 1994.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1023-1037
    • Benedetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 40
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida, J., Kraus, M. H., Alimandi, M., Di Fiore, P. P., and Carpenter, G. All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. J. Biol. Chem., 271: 5251-5257, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.