메뉴 건너뛰기




Volumn 16, Issue 7, 1997, Pages 1565-1574

Specific role for the PH domain of dynamin-1 in the regulation of rapid endocytosis in adrenal chromaffin cells

Author keywords

Chromaffin cells; Dynamin; Endocytosis; PH domain

Indexed keywords

DYNAMIN; ISOPROTEIN; PLECKSTRIN;

EID: 0030939005     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.7.1565     Document Type: Article
Times cited : (70)

References (51)
  • 2
    • 0030063683 scopus 로고    scopus 로고
    • Calmodulin is the divalent cation receptor for rapid endocytosis, but not exocytosis, in adrenal chromaffin cells
    • Artalejo,C.R., Elhamdani,A. and Palfrey,H.C. (1996) Calmodulin is the divalent cation receptor for rapid endocytosis, but not exocytosis, in adrenal chromaffin cells. Neuron, 16, 195-205.
    • (1996) Neuron , vol.16 , pp. 195-205
    • Artalejo, C.R.1    Elhamdani, A.2    Palfrey, H.C.3
  • 6
    • 0027310309 scopus 로고
    • Proteolytic fragments of phosphoinositide-specific PLCδ1. Catalytic and membrane-binding properties
    • Cifuentes,M.E., Honkanen,L. and Rebecchi,M.J. (1993) Proteolytic fragments of phosphoinositide-specific PLCδ1. Catalytic and membrane-binding properties. J. Biol. Chem., 268, 11586-11593.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11586-11593
    • Cifuentes, M.E.1    Honkanen, L.2    Rebecchi, M.J.3
  • 7
    • 0028137796 scopus 로고
    • Identification of dynamin-2, an isoform ubiquitously expressed in rat tissues
    • Cook,T.A., Urrutia,R. and McNiven,M.A. (1994) Identification of dynamin-2, an isoform ubiquitously expressed in rat tissues. Proc. Natl Acad. Sci. USA, 91, 644-648.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 644-648
    • Cook, T.A.1    Urrutia, R.2    McNiven, M.A.3
  • 8
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic vesicle formation
    • Damke,H., Baba,T., Warnock,D.E. and Schmid,S. (1994) Induction of mutant dynamin specifically blocks endocytic vesicle formation. J. Cell Biol., 127, 915-922.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-922
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.4
  • 9
    • 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 DeCamilli,P. (1996) 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) Proc. Natl Acad. Sci. USA , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    DeCamilli, P.4
  • 10
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin
    • Ferguson,K.M., Lemmon,M.A., Schlessinger,J. and Sigler,P.B. (1994) Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamin. Cell, 79, 199-209.
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 12
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson,K.M., Lemmon,M.A., Schlessinger,J. and Sigler,P.B. (1995b) Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell, 83, 1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 13
    • 0028836020 scopus 로고
    • Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy
    • Fushman,D., Cahill,S., Lemmon,M.A., Schlessinger,J. and Cowburn,D. (1995) Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy. Proc. Nail Acad. Sci. USA, 92, 816-820.
    • (1995) Proc. Nail Acad. Sci. USA , vol.92 , pp. 816-820
    • Fushman, D.1    Cahill, S.2    Lemmon, M.A.3    Schlessinger, J.4    Cowburn, D.5
  • 14
    • 0028787055 scopus 로고
    • The pleckstrin homology domain of phospholipase Cδ1 binds with high affinity to phosphatidylinositol-4,5-bisphosphate in bilayer membranes
    • Garcia,P., Gupta,R., Shah,S., Morris,A.J., Rudge,S.A., Scarlata,S., Petrova,V., McLaughlin,S. and Rebecchi,M.J. (1995) The pleckstrin homology domain of phospholipase Cδ1 binds with high affinity to phosphatidylinositol-4,5-bisphosphate in bilayer membranes. Biochemistry, 34, 16228-16234.
    • (1995) Biochemistry , vol.34 , pp. 16228-16234
    • Garcia, P.1    Gupta, R.2    Shah, S.3    Morris, A.J.4    Rudge, S.A.5    Scarlata, S.6    Petrova, V.7    McLaughlin, S.8    Rebecchi, M.J.9
  • 16
    • 0027362241 scopus 로고
    • The GTPase dynamin binds to and is activated by a subset of SH3 domains
    • Gout,I. et al. (1993) The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell, 75, 25-36.
    • (1993) Cell , vol.75 , pp. 25-36
    • Gout, I.1
  • 17
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4, 5-hisphosphate
    • Harlan,J.E., Hajduk,P.J., Yoon,H.S. and Fesik,S.W. (1994) Pleckstrin homology domains bind to phosphatidylinositol-4, 5-hisphosphate. Nature, 371, 168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 18
    • 0030176313 scopus 로고    scopus 로고
    • Fast steps in exocytosis and endocytosis studied by capacitance methods in endocrine cells
    • Henkel,A.W. and Almers,W. (1996) Fast steps in exocytosis and endocytosis studied by capacitance methods in endocrine cells. Curr. Opin. Neurobiol., 6, 350-357.
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 350-357
    • Henkel, A.W.1    Almers, W.2
  • 20
    • 0027133450 scopus 로고
    • Microtubules and src-homology 3 domains stimulate the dynamin GTPase via its C-terminal domain
    • Herskovits,J.S., Shpetner,H.S., Burgess,C.C. and Vallee,R.B. (1993b) Microtubules and src-homology 3 domains stimulate the dynamin GTPase via its C-terminal domain. Proc. Natl Acad. Sci. USA, 90, 11468-11472.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11468-11472
    • Herskovits, J.S.1    Shpetner, H.S.2    Burgess, C.C.3    Vallee, R.B.4
  • 22
    • 0020807636 scopus 로고
    • Reversible blockage of membrane retrieval and endocytosis in the garland cell of the temperature-sensitive mutant of Drosophila melanogaster, shibire
    • Kosaka,T. and Ikeda,K. (1983) Reversible blockage of membrane retrieval and endocytosis in the garland cell of the temperature-sensitive mutant of Drosophila melanogaster, shibire. J. Cell Biol., 97, 499-507.
    • (1983) J. Cell Biol. , vol.97 , pp. 499-507
    • Kosaka, T.1    Ikeda, K.2
  • 23
    • 0028874438 scopus 로고
    • Specific and high affinity binding of inositol phospholipids to an isolated pleckstrin homology domain
    • Lemmon,M.A., Ferguson,K.M., Sigler,P.B. and Schlessinger,J. (1995) Specific and high affinity binding of inositol phospholipids to an isolated pleckstrin homology domain. Proc. Natl Acad. Sci. USA, 92, 10472-10476.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    Sigler, P.B.3    Schlessinger, J.4
  • 24
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signalling molecules to the cell surface
    • Lemmon,M.A., Ferguson,K.M. and Schlessinger,J. (1996) PH domains: diverse sequences with a common fold recruit signalling molecules to the cell surface. Cell, 85, 621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 26
    • 0029029153 scopus 로고
    • Functional roles for the pleckstrin and Dbl homology regions in the Ras exchange factor Son-ofsevenless
    • McCollam,L., Bonfini,L., Karlovich,C.A., Conway,B.R., Kozma,L.M., Banerjee,U. and Czech,M.P. (1995) Functional roles for the pleckstrin and Dbl homology regions in the Ras exchange factor Son-ofsevenless. J. Biol. Chem., 270, 15954-15957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15954-15957
    • McCollam, L.1    Bonfini, L.2    Karlovich, C.A.3    Conway, B.R.4    Kozma, L.M.5    Banerjee, U.6    Czech, M.P.7
  • 28
    • 0027155543 scopus 로고
    • A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis
    • Nakata,T., Takemura,R. and Hirokawa,N. (1993) A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis. J. Cell Sci., 105, 1-5.
    • (1993) J. Cell Sci. , vol.105 , pp. 1-5
    • Nakata, T.1    Takemura, R.2    Hirokawa, N.3
  • 29
    • 0027229537 scopus 로고
    • Localization of dynamin: Widespread distribution in neurons and association with membranous organelles
    • Noda,Y., Nakata,T. and Hirokawa,N. (1993) Localization of dynamin: widespread distribution in neurons and association with membranous organelles. Neuroscience, 55, 113-127.
    • (1993) Neuroscience , vol.55 , pp. 113-127
    • Noda, Y.1    Nakata, T.2    Hirokawa, N.3
  • 30
    • 0025006964 scopus 로고
    • Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins
    • Obar,R.A., Collins,C.A., Hammarback,J.A., Shpetner,H.S. and Vallee,R.B. (1990) Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature, 347, 256-261.
    • (1990) Nature , vol.347 , pp. 256-261
    • Obar, R.A.1    Collins, C.A.2    Hammarback, J.A.3    Shpetner, H.S.4    Vallee, R.B.5
  • 31
    • 0028113779 scopus 로고
    • Calcium-triggered exocytosis and endocytosis in an isolated presynaptic cell: Capacitance measurements in saccular hair cells
    • Parsons,T.D., Lenzi,D., Almers,W. and Roberts,W.M. (1994) Calcium-triggered exocytosis and endocytosis in an isolated presynaptic cell: capacitance measurements in saccular hair cells. Neuron, 13, 875-883.
    • (1994) Neuron , vol.13 , pp. 875-883
    • Parsons, T.D.1    Lenzi, D.2    Almers, W.3    Roberts, W.M.4
  • 32
    • 0028847620 scopus 로고
    • Dephosphin/dynamin is a neuronal phosphoprotein concentrated in nerve terminals: Evidence from the cerebellum
    • Powell,K.A. and Robinson,P.J. (1995) Dephosphin/dynamin is a neuronal phosphoprotein concentrated in nerve terminals: evidence from the cerebellum. Neuroscience, 64, 821-833.
    • (1995) Neuroscience , vol.64 , pp. 821-833
    • Powell, K.A.1    Robinson, P.J.2
  • 35
    • 0025605785 scopus 로고
    • Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro
    • Scaife,R. and Margolis,R.L. (1990) Biochemical and immunochemical analysis of rat brain dynamin interaction with microtubules and organelles in vivo and in vitro. J. Cell Biol., 111, 3023-3033.
    • (1990) J. Cell Biol. , vol.111 , pp. 3023-3033
    • Scaife, R.1    Margolis, R.L.2
  • 36
    • 0028363432 scopus 로고
    • Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences
    • Scaife,R., Gout,I., Waterfield,M. and Margolis,R.L. (1994) Growth factor-induced binding of dynamin to signal transduction proteins involves sorting to distinct and separate proline-rich dynamin sequences. EMBO J., 13, 2574-2582.
    • (1994) EMBO J. , vol.13 , pp. 2574-2582
    • Scaife, R.1    Gout, I.2    Waterfield, M.3    Margolis, R.L.4
  • 37
    • 0026530775 scopus 로고
    • Dynamin is a GTPase stimulated to high levels of activity by microtubules
    • Shpetner,H. and Vallee,R.B. (1992) Dynamin is a GTPase stimulated to high levels of activity by microtubules. Nature, 355, 733-736.
    • (1992) Nature , vol.355 , pp. 733-736
    • Shpetner, H.1    Vallee, R.B.2
  • 39
    • 0028299459 scopus 로고
    • A triggered mechanism retrieves membrane in seconds after Ca-stimulated exocytosis in single pituitary cells
    • Thomas,P., Lee,A.K., Wong,J.G. and Almers,W. (1994) A triggered mechanism retrieves membrane in seconds after Ca-stimulated exocytosis in single pituitary cells. J. Cell Biol., 124, 667-676.
    • (1994) J. Cell Biol. , vol.124 , pp. 667-676
    • Thomas, P.1    Lee, A.K.2    Wong, J.G.3    Almers, W.4
  • 41
    • 0028246440 scopus 로고
    • Binding of G protein βγ-subunits to pleckstrin homology domains
    • Touhara,K., Inglese,J., Pitcher,J.A., Shaw,G. and Lefkowitz,R.J. (1994) Binding of G protein βγ-subunits to pleckstrin homology domains. J. Biol Chem., 269, 10217-10220.
    • (1994) J. Biol Chem. , vol.269 , pp. 10217-10220
    • Touhara, K.1    Inglese, J.2    Pitcher, J.A.3    Shaw, G.4    Lefkowitz, R.J.5
  • 42
    • 0028784414 scopus 로고
    • Dynamin forms polymeric complexes in the presence of lipid vesicles
    • Tuma,P.L. and Collins,C.A. (1995) Dynamin forms polymeric complexes in the presence of lipid vesicles. J. Biol. Chem., 270, 26707-26714.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26707-26714
    • Tuma, P.L.1    Collins, C.A.2
  • 43
    • 0028833412 scopus 로고
    • The regulation of endocytosis: Identifying dynamin's binding partners
    • Vallee,R.B. and Okamoto,P.M. (1995) The regulation of endocytosis: identifying dynamin's binding partners. Trends Cell Biol., 5, 43-47.
    • (1995) Trends Cell Biol. , vol.5 , pp. 43-47
    • Vallee, R.B.1    Okamoto, P.M.2
  • 44
    • 0025810110 scopus 로고
    • Dynamin-like protein encoded by the Drosophila shibire gene product associated with vesicular traffic
    • van der Bliek,A.M. and Meyerowitz,E.M. (1991) Dynamin-like protein encoded by the Drosophila shibire gene product associated with vesicular traffic. Nature, 351, 411-114.
    • (1991) Nature , vol.351 , pp. 411-1114
    • Van Der Bliek, A.M.1    Meyerowitz, E.M.2
  • 47
    • 0028082406 scopus 로고
    • Dynamics of synaptic vesicle fusion and membrane retrieval in synaptic terminals
    • von Gersdorff,H. and Matthews,G. (1994) Dynamics of synaptic vesicle fusion and membrane retrieval in synaptic terminals. Nature, 367, 735-739.
    • (1994) Nature , vol.367 , pp. 735-739
    • Von Gersdorff, H.1    Matthews, G.2
  • 49
    • 0029978885 scopus 로고    scopus 로고
    • Identification of the binding site for acidic phospholipids on the PH domain of dynamin: Implications for stimulation of GTPase activity
    • Zheng,J., Cahill,S., Lemmon,M.A., Fushman,D., Schlessinger,J. and Cowburn,D. (1996a) Identification of the binding site for acidic phospholipids on the PH domain of dynamin: implications for stimulation of GTPase activity. J. Mol. Biol., 255, 14-21.
    • (1996) J. Mol. Biol. , vol.255 , pp. 14-21
    • Zheng, J.1    Cahill, S.2    Lemmon, M.A.3    Fushman, D.4    Schlessinger, J.5    Cowburn, D.6
  • 50
    • 0029783037 scopus 로고    scopus 로고
    • The pleckstrin homology domain mediates transformation by oncogenic Dbl through specific intracellular targeting
    • Zheng,Y., Zangrilli,D., Cerione,R.A. and Eva,A. (1996b) The pleckstrin homology domain mediates transformation by oncogenic Dbl through specific intracellular targeting. J. Biol. Chem., 271, 19017-19020.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19017-19020
    • Zheng, Y.1    Zangrilli, D.2    Cerione, R.A.3    Eva, A.4
  • 51
    • 0028860968 scopus 로고
    • Structure and ligand recognition of the phosphotyrosine binding domain of Shc
    • Zhou,M.-M. et al. (1995) Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature, 378, 584-592.
    • (1995) Nature , vol.378 , pp. 584-592
    • Zhou, M.-M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.