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Volumn 14, Issue 7, 2003, Pages 2935-2945

Essential role of Ca2+/calmodulin in early endosome antigen-1 localization

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CALCIUM; CALMODULIN; CELL ANTIGEN; EARLY ENDOSOME ANTIGEN 1; LIPOSOME; PHOSPHATIDYLINOSITOL 3 KINASE; POLYPHOSPHOINOSITIDE; RAB PROTEIN; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; N (6 AMINOHEXYL) 1 NAPHTHALENESULFONAMIDE; N-(6-AMINOHEXYL)-1-NAPHTHALENESULFONAMIDE; RECOMBINANT PROTEIN; SULFONAMIDE; VESICULAR TRANSPORT PROTEIN;

EID: 0038784437     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-09-0591     Document Type: Article
Times cited : (31)

References (37)
  • 1
    • 0028304457 scopus 로고
    • The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in Madin-Darby canine kidney cells
    • Apodaca, G., Enrich, C., and Mostov, K.E. (1994). The calmodulin antagonist, W-13, alters transcytosis, recycling, and the morphology of the endocytic pathway in Madin-Darby canine kidney cells. J. Biol. Chem. 269, 19005-19013.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19005-19013
    • Apodaca, G.1    Enrich, C.2    Mostov, K.E.3
  • 2
    • 0028978947 scopus 로고
    • Distinct effects of alpha-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis
    • Chamberlain, L.H., Roth, D., Morgan, A., and Burgoyne, R.D. (1995). Distinct effects of alpha-SNAP, 14-3-3 proteins, and calmodulin on priming and triggering of regulated exocytosis. J. Cell Biol. 130, 1063-1070.
    • (1995) J. Cell Biol. , vol.130 , pp. 1063-1070
    • Chamberlain, L.H.1    Roth, D.2    Morgan, A.3    Burgoyne, R.D.4
  • 5
    • 0030944210 scopus 로고    scopus 로고
    • Calmodulin regulates endosome fusion
    • Colombo, M.I., Beron, W., and Stahl, P.D. (1997). Calmodulin regulates endosome fusion. J. Biol. Chem. 272, 7707-7712.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7707-7712
    • Colombo, M.I.1    Beron, W.2    Stahl, P.D.3
  • 6
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis, S., McBride, H.M., Burgoyne, R.D., and Zerial, M. (1999). The Rab5 effector EEA1 is a core component of endosome docking. Nature 397, 621-625.
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 8
    • 0034743311 scopus 로고    scopus 로고
    • PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox)
    • Ellson, C.D., et al. (2001). PtdIns(3)P regulates the neutrophil oxidase complex by binding to the PX domain of p40(phox). Nat. Cell Biol. 3, 679-682.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 679-682
    • Ellson, C.D.1
  • 10
    • 0023767794 scopus 로고
    • A 115 kDa calmodulin-binding protein is located in rat liver endosome fractions
    • Enrich, C., Bachs, O., and Evans, W.H. (1988). A 115 kDa calmodulin-binding protein is located in rat liver endosome fractions. Biochem. J. 255, 999-1005.
    • (1988) Biochem. J. , vol.255 , pp. 999-1005
    • Enrich, C.1    Bachs, O.2    Evans, W.H.3
  • 11
    • 0025974686 scopus 로고
    • rab5 controls early endosome fusion in vitro
    • Gorvel, J.P., Chavrier, P., Zerial, M., and Gruenberg, J. (1991). rab5 controls early endosome fusion in vitro. Cell 64, 915-925.
    • (1991) Cell , vol.64 , pp. 915-925
    • Gorvel, J.P.1    Chavrier, P.2    Zerial, M.3    Gruenberg, J.4
  • 12
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K.P., and Ikura, M. (2002). Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108, 739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 13
    • 0032824099 scopus 로고    scopus 로고
    • Fusion of endosomes involved in synaptic vesicle recycling
    • Holroyd, C., Kistner, U., Annaert, W., and Jahn, R. (1999). Fusion of endosomes involved in synaptic vesicle recycling. Mol. Biol. Cell. 10, 3035-3044.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3035-3044
    • Holroyd, C.1    Kistner, U.2    Annaert, W.3    Jahn, R.4
  • 14
    • 0034208540 scopus 로고    scopus 로고
    • Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells
    • Huber, L.A., Fialka, I., Paiha, K., Hunziker, W., Sacks, D.B., Bahler, M., Way, M., Gagescu, R., and Gruenberg, J. (2000). Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells. Traffic 1, 494-503.
    • (2000) Traffic , vol.1 , pp. 494-503
    • Huber, L.A.1    Fialka, I.2    Paiha, K.3    Hunziker, W.4    Sacks, D.B.5    Bahler, M.6    Way, M.7    Gagescu, R.8    Gruenberg, J.9
  • 15
    • 0023026101 scopus 로고
    • Calcium-binding proteins and secretion
    • Hutton, J.C. (1986). Calcium-binding proteins and secretion. Cell Calcium 7, 339-352.
    • (1986) Cell Calcium , vol.7 , pp. 339-352
    • Hutton, J.C.1
  • 17
  • 18
    • 0032537835 scopus 로고    scopus 로고
    • Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes
    • Mills, I.G., Jones, A.T., and Clague, M.J. (1998). Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes. Curr. Biol. 8, 881-884.
    • (1998) Curr. Biol. , vol.8 , pp. 881-884
    • Mills, I.G.1    Jones, A.T.2    Clague, M.J.3
  • 20
    • 0034988109 scopus 로고    scopus 로고
    • Relationships between EEA1 binding partners and their role in endosome fusion
    • Mills, I.G., Urbe, S., and Clague, M.J. (2001). Relationships between EEA1 binding partners and their role in endosome fusion. J. Cell Sci. 114, 1959-1965.
    • (2001) J. Cell Sci. , vol.114 , pp. 1959-1965
    • Mills, I.G.1    Urbe, S.2    Clague, M.J.3
  • 21
    • 0029030937 scopus 로고
    • EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif
    • Mu, F.T., Callaghan, J.M., Steele-Mortimer, O., Stenmark, H., Parton, R.G., Campbell, P.L., McCluskey, J., Yeo, J.P., Tock, E.P., and Toh, B.H. (1995). EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif. J. Biol. Chem. 270, 13503-13511.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13503-13511
    • Mu, F.T.1    Callaghan, J.M.2    Steele-Mortimer, O.3    Stenmark, H.4    Parton, R.G.5    Campbell, P.L.6    McCluskey, J.7    Yeo, J.P.8    Tock, E.P.9    Toh, B.H.10
  • 22
    • 0019986619 scopus 로고
    • Role of calmodulin in platelet aggregation. Structure-activity relationship of calmodulin antagonists
    • Nishikawa, M., and Hidaka, H. (1982). Role of calmodulin in platelet aggregation. Structure-activity relationship of calmodulin antagonists. J. Clin. Investig. 69, 1348-1355.
    • (1982) J. Clin. Investig. , vol.69 , pp. 1348-1355
    • Nishikawa, M.1    Hidaka, H.2
  • 24
    • 0032506349 scopus 로고    scopus 로고
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396, 575-580.
    • (1998) Nature , vol.396 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 25
    • 0034729167 scopus 로고    scopus 로고
    • The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • Pryor, P.R., Mullock, B.M., Bright, N.A., Gray, S.R., and Luzio, J.P. (2000). The role of intraorganellar Ca(2+) in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. 149, 1053-1062.
    • (2000) J. Cell Biol. , vol.149 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 26
    • 0035432383 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis: Here today, and here tomorrow
    • Russell, D.G. (2001). Mycobacterium tuberculosis: here today, and here tomorrow. Nat. Rev. Mol. Cell. Biol. 2, 569-577.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 569-577
    • Russell, D.G.1
  • 27
    • 0028232699 scopus 로고
    • Alteration of calmodulin-protein interactions by a monoclonal antibody to calmodulin
    • Sacks, D.B. (1994). Alteration of calmodulin-protein interactions by a monoclonal antibody to calmodulin. Biochim. Biophys. Acta 1206, 120-128.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 120-128
    • Sacks, D.B.1
  • 29
    • 0032517624 scopus 로고    scopus 로고
    • Distinct roles for the p110alpha and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton, and mitogenesis
    • Siddhanta, U., McIlroy, J., Shah, A., Zhang, Y., and Backer, J.M. (1998). Distinct roles for the p110alpha and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton, and mitogenesis. J. Cell Biol. 143, 1647-1659.
    • (1998) J. Cell Biol. , vol.143 , pp. 1647-1659
    • Siddhanta, U.1    McIlroy, J.2    Shah, A.3    Zhang, Y.4    Backer, J.M.5
  • 32
    • 0030027394 scopus 로고    scopus 로고
    • Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin
    • Shpetner, H., Joly, M., Hartley, D., and Corvera, S. (1996). Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin. J. Cell Biol. 132, 595-605.
    • (1996) J. Cell Biol. , vol.132 , pp. 595-605
    • Shpetner, H.1    Joly, M.2    Hartley, D.3    Corvera, S.4
  • 33
    • 0029846518 scopus 로고    scopus 로고
    • Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger
    • Stenmark, H., Aasland, R., Toh, B.-H., and D'Arrigo, A. (1996). Endosomal localization of the autoantigen EEA1 is mediated by a zinc-binding FYVE finger. J. Biol. Chem. 271, 24048-24054.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24048-24054
    • Stenmark, H.1    Aasland, R.2    Toh, B.-H.3    D'Arrigo, A.4
  • 34
    • 0029884657 scopus 로고    scopus 로고
    • Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain
    • Virbasius, J.V., Guilherme, A., and Czech, M.P. (1996). Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain. J. Biol. Chem. 271, 13304-13307.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13304-13307
    • Virbasius, J.V.1    Guilherme, A.2    Czech, M.P.3
  • 35
    • 0035818611 scopus 로고    scopus 로고
    • Activation of the Akt-related cytokine-independent survival kinase requires interaction of its phox domain with endosomal phosphatidylinositol 3-phosphate
    • Virbasius, J.V., Song, X., Pomerleau, D.P., Zhan, Y., Zhou, G.W., and Czech, M.P. (2001). Activation of the Akt-related cytokine-independent survival kinase requires interaction of its phox domain with endosomal phosphatidylinositol 3-phosphate. Proc. Natl. Acad. Sci. USA 98, 12908-12913.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12908-12913
    • Virbasius, J.V.1    Song, X.2    Pomerleau, D.P.3    Zhan, Y.4    Zhou, G.W.5    Czech, M.P.6
  • 36
    • 0034944422 scopus 로고    scopus 로고
    • SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P
    • Xu, Y., Hortsman, H., Seet, L., Wong, S.H., and Hong, W. (2001). SNX3 regulates endosomal function through its PX-domain-mediated interaction with PtdIns(3)P. Nat. Cell Biol. 3, 658-666.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 658-666
    • Xu, Y.1    Hortsman, H.2    Seet, L.3    Wong, S.H.4    Hong, W.5
  • 37
    • 0035941208 scopus 로고    scopus 로고
    • All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate
    • Yu, J.W., and Lemmon, M.A. (2001). All phox homology (PX) domains from Saccharomyces cerevisiae specifically recognize phosphatidylinositol 3-phosphate. J. Biol. Chem. 276, 44179-44184.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44179-44184
    • Yu, J.W.1    Lemmon, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.