메뉴 건너뛰기




Volumn 10, Issue 8, 2000, Pages 471-474

Direct interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS;

EID: 0034176612     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00446-2     Document Type: Article
Times cited : (66)

References (27)
  • 2
    • 0029773891 scopus 로고    scopus 로고
    • Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties
    • Ramjaun A.R., McPherson P.S. Tissue-specific alternative splicing generates two synaptojanin isoforms with differential membrane binding properties. J Biol Chem. 271:1996;24856-24861.
    • (1996) J Biol Chem , vol.271 , pp. 24856-24861
    • Ramjaun, A.R.1    McPherson, P.S.2
  • 3
    • 0030981640 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments
    • Sakisaka T., Itoh T., Miura K., Takenawa T. Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments. Mol Cell Biol. 17:1997;3841-3849.
    • (1997) Mol Cell Biol , vol.17 , pp. 3841-3849
    • Sakisaka, T.1    Itoh, T.2    Miura, K.3    Takenawa, T.4
  • 4
    • 0345646448 scopus 로고    scopus 로고
    • Synaptojanin family members are implicated in endocytic membrane traffic in yeast
    • Singer-Kruger B., Nemoto Y., Daniell L., Ferro-Novick S., De Camilli P. Synaptojanin family members are implicated in endocytic membrane traffic in yeast. J Cell Sci. 111:1998;3347-3356.
    • (1998) J Cell Sci , vol.111 , pp. 3347-3356
    • Singer-Kruger, B.1    Nemoto, Y.2    Daniell, L.3    Ferro-Novick, S.4    De Camilli, P.5
  • 5
    • 0032736675 scopus 로고    scopus 로고
    • Essential role of phosphoinositide metabolism in synaptic vesicle recycling
    • Cremona O., Di Paolo G., Wenk M.R., Luthi A., Kim W.T., Takei K.et al. Essential role of phosphoinositide metabolism in synaptic vesicle recycling. Cell. 99:1999;179-188.
    • (1999) Cell , vol.99 , pp. 179-188
    • Cremona, O.1    Di Paolo, G.2    Wenk, M.R.3    Luthi, A.4    Kim, W.T.5    Takei, K.6
  • 6
    • 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.et al. Synaptojanin 1. localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15 FEBS Lett. 419:1997;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
  • 7
    • 0033532062 scopus 로고    scopus 로고
    • SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
    • Guo S., Stolz L.E., Lemrow S.M., York J.D. SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases. J Biol Chem. 274:1999;12990-12995.
    • (1999) J Biol Chem , vol.274 , pp. 12990-12995
    • Guo, S.1    Stolz, L.E.2    Lemrow, S.M.3    York, J.D.4
  • 8
    • 0024828304 scopus 로고
    • Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function
    • Cleves A.E., Novick P.J., Bankaitis V.A. Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function. J Cell Biol. 109:1989;2939-2950.
    • (1989) J Cell Biol , vol.109 , pp. 2939-2950
    • Cleves, A.E.1    Novick, P.J.2    Bankaitis, V.A.3
  • 9
    • 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., De Camilli 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 USA. 94:1997;8569-8574.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8569-8574
    • Ringstad, N.1    Nemoto, Y.2    De Camilli, P.3
  • 11
    • 0032563187 scopus 로고    scopus 로고
    • Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin
    • Roos J., Kelly R.B. Dap160, a neural-specific Eps15 homology and multiple SH3 domain-containing protein that interacts with Drosophila dynamin. J Biol Chem. 273:1998;19108-19119.
    • (1998) J Biol Chem , vol.273 , pp. 19108-19119
    • Roos, J.1    Kelly, R.B.2
  • 12
    • 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., 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
  • 13
    • 0030930853 scopus 로고    scopus 로고
    • Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module
    • Salcini A.E., Confalonieri S., Doria M., Santolini E., Tassi E., Minenkova O.et al. Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module. Genes Dev. 11:1997;2239-2249.
    • (1997) Genes Dev , vol.11 , pp. 2239-2249
    • Salcini, A.E.1    Confalonieri, S.2    Doria, M.3    Santolini, E.4    Tassi, E.5    Minenkova, O.6
  • 14
    • 15844361829 scopus 로고    scopus 로고
    • The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein
    • Benmerah A., Begue B., Dautry-Varsat A., Cerf-Bensussan N. The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein. J Biol Chem. 271:1996;12111-12116.
    • (1996) J Biol Chem , vol.271 , pp. 12111-12116
    • Benmerah, A.1    Begue, B.2    Dautry-Varsat, A.3    Cerf-Bensussan, N.4
  • 16
    • 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., Kirchhausen T. Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits. J Biol Chem. 271:1996;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
  • 17
    • 0028986797 scopus 로고
    • The appendage domain of alpha-adaptin is a high affinity binding site for dynamin
    • Wang L.H., Südhof T.C., Anderson R.G.W. The appendage domain of alpha-adaptin is a high affinity binding site for dynamin. J Biol Chem. 270:1995;10079-10083.
    • (1995) J Biol Chem , vol.270 , pp. 10079-10083
    • Wang, L.H.1    Südhof, T.C.2    Anderson, R.G.W.3
  • 18
    • 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., 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. 93:1996;331-335.
    • (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
  • 19
    • 0032552056 scopus 로고    scopus 로고
    • Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
    • Chen H., Fre S., Slepnev V.I., Capua M.R., Takei K., Butler M.H.et al. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature. 394:1998;793-797.
    • (1998) Nature , vol.394 , pp. 793-797
    • Chen, H.1    Fre, S.2    Slepnev, V.I.3    Capua, M.R.4    Takei, K.5    Butler, M.H.6
  • 20
    • 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., Dafforn T.R., Evans P.R.et al. A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain. Cell. 97:1999;805-815.
    • (1999) Cell , vol.97 , pp. 805-815
    • Owen, D.J.1    Vallis, Y.2    Noble, M.E.3    Hunter, J.B.4    Dafforn, T.R.5    Evans, P.R.6
  • 21
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman O.B. Jr., Krupnick J.G., Gurevich V.V., Benovic J.L., Keen J.H. Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J Biol Chem. 272:1997;15017-15022.
    • (1997) J Biol Chem , vol.272 , pp. 15017-15022
    • Goodman O.B., Jr.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 23
    • 0032514995 scopus 로고    scopus 로고
    • Atomic structure of clathrin: A beta propeller terminal domain joins an alpha zigzag linker
    • ter Haar E., Musacchio A., Harrison S.C., Kirchhausen T. Atomic structure of clathrin. a beta propeller terminal domain joins an alpha zigzag linker Cell. 95:1998;563-573.
    • (1998) Cell , vol.95 , pp. 563-573
    • Ter Haar, E.1    Musacchio, A.2    Harrison, S.C.3    Kirchhausen, T.4
  • 24
    • 0029584896 scopus 로고
    • A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes
    • Shih W., Gallusser A., Kirchhausen T. A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes. J Biol Chem. 270:1995;31083-31090.
    • (1995) J Biol Chem , vol.270 , pp. 31083-31090
    • Shih, W.1    Gallusser, A.2    Kirchhausen, T.3
  • 25
    • 0030792523 scopus 로고    scopus 로고
    • Clathrin interacts specifically with amphiphysin and is displaced by dynamin
    • McMahon H.T., Wigge P., 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
  • 26
    • 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.et al. 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
  • 27
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli P., Emr S.D., McPherson P.S., Novick P. Phosphoinositides as regulators in membrane traffic. Science. 271:1996;1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.