메뉴 건너뛰기




Volumn 17, Issue 22, 1998, Pages 6541-6550

Recognition specificity of individual EH domains of mammals and yeast

Author keywords

End3; Pan1; Phage display; Protein binding modules; YBL47C

Indexed keywords

PEPTIDE;

EID: 0032538882     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.22.6541     Document Type: Article
Times cited : (101)

References (35)
  • 2
    • 0028024386 scopus 로고
    • The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast
    • Benedetti, H., Raths, S., Crausaz, F. and Riezman, H. (1994) The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Mol. Biol. Cell, 5, 1023-1037.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1023-1037
    • Benedetti, H.1    Raths, S.2    Crausaz, F.3    Riezman, H.4
  • 3
    • 15844361829 scopus 로고    scopus 로고
    • The ear of α-adaptin interacts with the COOH-terminal domain of the Eps15 protein
    • Benmerah, A., Begue, B., Dautry-Varsat, A. and Cerf-Bensussan, N. (1996) The ear of α-adaptin interacts with the COOH-terminal domain of the Eps15 protein. J. Biol. Chem., 20, 12111-12116.
    • (1996) J. Biol. Chem. , vol.20 , pp. 12111-12116
    • Benmerah, A.1    Begue, B.2    Dautry-Varsat, A.3    Cerf-Bensussan, N.4
  • 7
    • 0032579263 scopus 로고    scopus 로고
    • Eps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalization
    • Coda, L., Salcini, A.E., Confalonieri, S., Pelicci, G., Sorkina, T., Sorkin, A., Pelicci, P.G. and Di Fiore, P.P. (1998) Eps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalization. J. Biol. Chem., 273, 3003-3012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3003-3012
    • Coda, L.1    Salcini, A.E.2    Confalonieri, S.3    Pelicci, G.4    Sorkina, T.5    Sorkin, A.6    Pelicci, P.G.7    Di Fiore, P.P.8
  • 8
    • 0032575695 scopus 로고    scopus 로고
    • Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain
    • de Beer, T., Carter, R.E., Lobel-Rice, K.E., Sorkin, A. and Overduin, M. (1998) Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science, 281, 1357-1360.
    • (1998) Science , vol.281 , pp. 1357-1360
    • De Beer, T.1    Carter, R.E.2    Lobel-Rice, K.E.3    Sorkin, A.4    Overduin, M.5
  • 9
    • 0021111813 scopus 로고
    • pEMBL: A new family of single stranded plasmids
    • Dente, L., Cesareni, G. and Cortese, R. (1983) pEMBL: a new family of single stranded plasmids. Nucleic Acids Res., 11, 1645-1655.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1645-1655
    • Dente, L.1    Cesareni, G.2    Cortese, R.3
  • 10
    • 0031588018 scopus 로고    scopus 로고
    • Modified phage peptide libraries as a tool to study specificity of phosphorylation and recognition of tyrosine containing peptides
    • Dente, L., Vetriani, V., Zucconi, A., Pelicci, G., Lanfrancone, L., Pelicci, P.G. and Cesareni, G. (1997) Modified phage peptide libraries as a tool to study specificity of phosphorylation and recognition of tyrosine containing peptides. J. Mol. Biol., 269, 694-703.
    • (1997) J. Mol. Biol. , vol.269 , pp. 694-703
    • Dente, L.1    Vetriani, V.2    Zucconi, A.3    Pelicci, G.4    Lanfrancone, L.5    Pelicci, P.G.6    Cesareni, G.7
  • 11
    • 0030663664 scopus 로고    scopus 로고
    • EH: A novel protein-protein interaction domain potentially in intracellular sorting
    • Di Fiore, P.P., Pelicci, P.G. and Sorkin, A. (1997) EH: a novel protein-protein interaction domain potentially in intracellular sorting. Trends Biochem. Sci., 22, 411-413.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 411-413
    • Di Fiore, P.P.1    Pelicci, P.G.2    Sorkin, A.3
  • 13
    • 0026411004 scopus 로고
    • Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector
    • Felici, F., Castagnoli, L., Musacchio, A., Jappelli, R. and Cesareni, G. (1991) Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector. J. Mol. Biol., 221, 301-310.
    • (1991) J. Mol. Biol. , vol.221 , pp. 301-310
    • Felici, F.1    Castagnoli, L.2    Musacchio, A.3    Jappelli, R.4    Cesareni, G.5
  • 14
    • 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., Butler, M.H., Salcini, A.E., Di Fiore, P.P. and De Camilli, P. (1997) Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. FEBS Lett., 419, 175-180.
    • (1997) FEBS Lett. , vol.419 , pp. 175-180
    • Haffner, C.1    Takei, K.2    Chen, H.3    Ringstad, N.4    Hudson, A.5    Butler, M.H.6    Salcini, A.E.7    Di Fiore, P.P.8    De Camilli, P.9
  • 16
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M. Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B. and Bax, A. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science, 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 17
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • Meador, W.E., Means, A.R. and Quiocho, F.A. (1992) Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science, 257, 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 18
    • 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. (1995) end5, end6 and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae. Mol. Biol. Cell, 6, 1721-1742.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1721-1742
    • Munn, A.L.1    Stevenson, B.J.2    Geli, M.I.3    Riezman, H.4
  • 19
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring and adaptor proteins
    • Pawson, T. and Scott, J.D. (1997) Signaling through scaffold, anchoring and adaptor proteins. Science, 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 20
    • 0027971687 scopus 로고
    • Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries
    • Rickles, R.J., Botfield, M.C., Weng, Z., Taylor, J.A., Green, O.M., Brugge, J.S. and Zoller, M.J. (1994) Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries. EMBO J., 13, 5598-5604.
    • (1994) EMBO J. , vol.13 , pp. 5598-5604
    • Rickles, R.J.1    Botfield, M.C.2    Weng, Z.3    Taylor, J.A.4    Green, O.M.5    Brugge, J.S.6    Zoller, M.J.7
  • 21
    • 0032563187 scopus 로고    scopus 로고
    • Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin
    • Roos, J., and Kelly, R.B. (1998) Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin. J. Biol. Chem., 273, 19108-19119.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19108-19119
    • Roos, J.1    Kelly, R.B.2
  • 23
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z. et al. (1993) SH2 domains recognize specific phosphopeptide sequences. Cell, 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 24
    • 0028351583 scopus 로고
    • Specific motifs recognised by the SH2 domains of Csk, 3BP2, fps/fes, Grb-2, HCP, SHC, Sykand Vav
    • Songyang, Z. et al. (1994) Specific motifs recognised by the SH2 domains of Csk, 3BP2, fps/fes, Grb-2, HCP, SHC, Sykand Vav. Mol. Cell. Biol., 14, 2777-2785.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2777-2785
    • Songyang, Z.1
  • 25
    • 15644379801 scopus 로고    scopus 로고
    • Recognition of unique C-terminal motifs by distinct PDZ domains
    • Songyang, Z. et al. (1997) Recognition of unique C-terminal motifs by distinct PDZ domains. Science, 275, 73-77.
    • (1997) Science , vol.275 , pp. 73-77
    • Songyang, Z.1
  • 26
    • 0027984955 scopus 로고
    • Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries
    • Sparks, A.B., Quilliam, L.A., Thorn, J.M., Der, C.J. and Kay, B.K. (1994) Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries. J. Biol. Chem., 269, 23853-23856.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23853-23856
    • Sparks, A.B.1    Quilliam, L.A.2    Thorn, J.M.3    Der, C.J.4    Kay, B.K.5
  • 27
    • 0030459065 scopus 로고    scopus 로고
    • The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae
    • Tan, P.K., Howard, J.P. and Payne, G.S. (1996) The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae. J. Cell Biol., 135, 1789-1800.
    • (1996) J. Cell Biol. , vol.135 , pp. 1789-1800
    • Tan, P.K.1    Howard, J.P.2    Payne, G.S.3
  • 28
    • 0029772320 scopus 로고    scopus 로고
    • The EH-domain-containing protein Pan1 is required for normal organisation of the actin cytoskeleton in Saccharomyces cerevisiae
    • Tang, H.Y. and Cai, M. (1996) The EH-domain-containing protein Pan1 is required for normal organisation of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Cell. Biol., 16, 4897-4914.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4897-4914
    • Tang, H.Y.1    Cai, M.2
  • 29
    • 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, H.Y., Munn, A. and 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, 4294-4304.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4294-4304
    • Tang, H.Y.1    Munn, A.2    Cai, M.3
  • 30
    • 0029826531 scopus 로고    scopus 로고
    • Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits
    • Tebar, F., Sorkina, T., Sorkin, A., Ericsson, M. and Kirchhausen, T. (1996) Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits. J. Biol. Chem., 271, 28727-28730.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28727-28730
    • Tebar, F.1    Sorkina, T.2    Sorkin, A.3    Ericsson, M.4    Kirchhausen, T.5
  • 32
    • 0032489873 scopus 로고    scopus 로고
    • Pan1p, Yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis
    • Wendland, B. and Emr, S.D. (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
  • 35
    • 0031465736 scopus 로고    scopus 로고
    • An Eps homology (EH) domain that binds to the Ral-GTPase, Ra1BP1
    • Yamaguchi, A., Urano, T., Goi, T. and Feig, L.A. (1997) An Eps homology (EH) domain that binds to the Ral-GTPase, Ra1BP1. J. Biol. Chem., 272, 31230-31234.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31230-31234
    • Yamaguchi, A.1    Urano, T.2    Goi, T.3    Feig, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.