메뉴 건너뛰기




Volumn 21, Issue 22, 2002, Pages 6125-6135

Rab-αGDI activity is regulated by a Hsp90 chaperone complex

Author keywords

CSP; GDI; Hsp90; Rab3A; Synaptic vesicle

Indexed keywords

CALCIUM; CHAPERONE; CYSTEINE STRING PROTEIN; GELDANAMYCIN; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANOSINE TRIPHOSPHATASE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN 90; RAB PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; AGENTS INTERACTING WITH TRANSMITTER, HORMONE OR DRUG RECEPTORS; BENZOQUINONE DERIVATIVE; GDP DISSOCIATION INHIBITOR 1; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HSPA8 PROTEIN, RAT; LACTONE; MACROCYCLIC LACTAM; MACROLIDE; MEMBRANE PROTEIN; NERVE PROTEIN; QUINONE DERIVATIVE; RADICICOL;

EID: 0037110754     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf603     Document Type: Article
Times cited : (94)

References (41)
  • 1
    • 0034898458 scopus 로고    scopus 로고
    • Organization of the Rab-GDI/CHM superfamily: The functional basis for choroideremia disease
    • Alory, C. and Balch, W.E. (2001) Organization of the Rab-GDI/CHM superfamily: The functional basis for choroideremia disease. Traffic, 2, 532-543.
    • (2001) Traffic , vol.2 , pp. 532-543
    • Alory, C.1    Balch, W.E.2
  • 2
    • 0026709643 scopus 로고
    • Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components
    • Bittner, M.A. and Holz, R.W. (1992) Kinetic analysis of secretion from permeabilized adrenal chromaffin cells reveals distinct components. J. Biol. Chem., 267, 16219-16225.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16219-16225
    • Bittner, M.A.1    Holz, R.W.2
  • 3
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch, G.L. and Lassle, M. (1999) The tetratricopeptide repeat: A structural motif mediating protein-protein interactions. BioEssays, 21, 932-939.
    • (1999) BioEssays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 5
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • Buchner, J. (1999) Hsp90 & Co. - A holding for folding. Trends Biochem. Sci., 24, 136-141.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 6
    • 0030051050 scopus 로고    scopus 로고
    • Synaptic vesicle biogenesis, docking and fusion: A molecular description
    • Calakos, N. and Scheller, R.H. (1996) Synaptic vesicle biogenesis, docking and fusion: A molecular description. Physiol. Rev., 76, 1-29.
    • (1996) Physiol. Rev. , vol.76 , pp. 1-29
    • Calakos, N.1    Scheller, R.H.2
  • 9
    • 0034051803 scopus 로고    scopus 로고
    • Cysteine-string protein: The chaperone at the synapse
    • Chamberlain, L.H. and Burgoyne, R.D. (2000) Cysteine-string protein: The chaperone at the synapse. J. Neurochem., 74, 1781-1789.
    • (2000) J. Neurochem. , vol.74 , pp. 1781-1789
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 10
    • 17344369362 scopus 로고    scopus 로고
    • Mutations in GDII are responsible for X-linked non-specific mental retardation
    • D'Adamo, P. et al. (1998) Mutations in GDII are responsible for X-linked non-specific mental retardation. Nat. Genet., 19, 134-139.
    • (1998) Nat. Genet. , vol.19 , pp. 134-139
    • D'Adamo, P.1
  • 12
    • 0031023505 scopus 로고    scopus 로고
    • Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI
    • Dirac-Svejstrup, A.B., Sumizawa, T. and Pfeffer, S.R. (1997) Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI. EMBO J., 16, 465-472.
    • (1997) EMBO J. , vol.16 , pp. 465-472
    • Dirac-Svejstrup, A.B.1    Sumizawa, T.2    Pfeffer, S.R.3
  • 13
    • 0031898897 scopus 로고    scopus 로고
    • RAB3 and synaptotagmin: The yin and yang of synaptic membrane fusion
    • Geppert, M. and Sudhof, T.C. (1998) RAB3 and synaptotagmin: The yin and yang of synaptic membrane fusion. Annu. Rev. Neurosci., 21, 75-95.
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 75-95
    • Geppert, M.1    Sudhof, T.C.2
  • 14
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Hohfeld, J., Minami, Y. and Hartl, F.U. (1995) Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell, 83, 589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Hohfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 15
    • 12944333135 scopus 로고    scopus 로고
    • Role of rab GDP dissociation inhibitor αin regulating plasticity of hippocampal neurotransmission
    • Ishizaki, H. et al. (2000) Role of rab GDP dissociation inhibitor αin regulating plasticity of hippocampal neurotransmission. Proc. Natl Acad. Sci. USA, 97, 11587-11592.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11587-11592
    • Ishizaki, H.1
  • 16
    • 0033591317 scopus 로고    scopus 로고
    • Molecular dissection of guanine nucleotide dissociation inhibitor function in vivo. Rab-independent binding to membranes and role of Rab recycling factors
    • Luan, P., Balch, W.E., Emr, S.D. and Burd, C.G. (1999) Molecular dissection of guanine nucleotide dissociation inhibitor function in vivo. Rab-independent binding to membranes and role of Rab recycling factors. J. Biol. Chem. 274, 14806-14817.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14806-14817
    • Luan, P.1    Balch, W.E.2    Emr, S.D.3    Burd, C.G.4
  • 17
    • 0034157347 scopus 로고    scopus 로고
    • A new functional domain of guanine nucleotide dissociation inhibitor α-GDI) involved in Rab recycling
    • Luan, P., Heine, A., Moyer, B.D., Greasely, S.E., Kuhn, P., Balch, W.E. and Wilson, I.A. (2000) A new functional domain of guanine nucleotide dissociation inhibitor α-GDI) involved in Rab recycling. Traffic, 1, 270-281.
    • (2000) Traffic , vol.1 , pp. 270-281
    • Luan, P.1    Heine, A.2    Moyer, B.D.3    Greasely, S.E.4    Kuhn, P.5    Balch, W.E.6    Wilson, I.A.7
  • 18
    • 0032544437 scopus 로고    scopus 로고
    • The effects of SNAP/SNARE complexes on the ATPase of NSF
    • Matveeva, E. and Whiteheart, S.W. (1998) The effects of SNAP/SNARE complexes on the ATPase of NSF. FEBS Lett., 435, 211-214.
    • (1998) FEBS Lett. , vol.435 , pp. 211-214
    • Matveeva, E.1    Whiteheart, S.W.2
  • 19
    • 0035950260 scopus 로고    scopus 로고
    • Uncoating of clathrin-coated vesicles in presynaptic terminals. Roles for hsc70 and auxilin
    • Morgan, J.R., Prasad, K., Jin, S., Augustine, G.J. and Lafer, E.M. (2001) Uncoating of clathrin-coated vesicles in presynaptic terminals. Roles for hsc70 and auxilin. Neuron, 32, 289-300.
    • (2001) Neuron , vol.32 , pp. 289-300
    • Morgan, J.R.1    Prasad, K.2    Jin, S.3    Augustine, G.J.4    Lafer, E.M.5
  • 20
    • 0035809183 scopus 로고    scopus 로고
    • Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo
    • Newmyer, S.L. and Schmid, S.L. (2001) Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo. J. Cell Biol., 152, 607-620.
    • (2001) J. Cell Biol. , vol.152 , pp. 607-620
    • Newmyer, S.L.1    Schmid, S.L.2
  • 21
    • 0022545785 scopus 로고
    • Synaptosomes possess an exocytotic pool of glutamate
    • Nicholls, D.G. and Sihra, T.S. (1986) Synaptosomes possess an exocytotic pool of glutamate. Nature, 321, 772-773.
    • (1986) Nature , vol.321 , pp. 772-773
    • Nicholls, D.G.1    Sihra, T.S.2
  • 22
    • 0035798385 scopus 로고    scopus 로고
    • Evolution of the Rab family of small GTP-binding proteins
    • Pereira-Leal, J.B. and Seabra, M.C. (2001) Evolution of the Rab family of small GTP-binding proteins. J. Mol. Biol., 313, 889-901.
    • (2001) J. Mol. Biol. , vol.313 , pp. 889-901
    • Pereira-Leal, J.B.1    Seabra, M.C.2
  • 23
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W. and Pearl, L.H. (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell, 90, 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 24
    • 0031916186 scopus 로고    scopus 로고
    • Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling
    • Ranjan, R., Bronk, P. and Zinsmaier, K.E. (1998) Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling. J. Neurosci., 18, 956-964.
    • (1998) J. Neurosci. , vol.18 , pp. 956-964
    • Ranjan, R.1    Bronk, P.2    Zinsmaier, K.E.3
  • 25
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: Chaperoning signal transduction
    • Richter, K. and Buchner, J. (2001) Hsp90: Chaperoning signal transduction. J. Cell Physiol., 188, 281-290.
    • (2001) J. Cell Physiol. , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 26
    • 0032959590 scopus 로고    scopus 로고
    • Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe, S.M., Prodromou, C., O'Brien, R., Ladbury, J.E., Piper, P.W. and Pearl, L.H. (1999) Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem., 42, 260-266.
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 30
    • 0029935431 scopus 로고    scopus 로고
    • Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by Ras
    • Stahl, B., Chou, J.H., Li, C., Sudhof, T.C. and Jahn, R. (1996) Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by Ras. EMBO J., 15, 1799-1809.
    • (1996) EMBO J. , vol.15 , pp. 1799-1809
    • Stahl, B.1    Chou, J.H.2    Li, C.3    Sudhof, T.C.4    Jahn, R.5
  • 31
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C.E., Russo, A.A., Schneider, C., Rosen, N., Hartl, F.U. and Pavletich, N.P. (1997) Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell, 89, 239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 33
    • 0032125862 scopus 로고    scopus 로고
    • Differential regulation of exocytosis by calcium and CAPS in semi-intact synaptosomes
    • Tandon, A., Bannykh, S., Kowalchyk, J.A., Banerjee, A., Martin, T.F. and Balch, W.E. (1998) Differential regulation of exocytosis by calcium and CAPS in semi-intact synaptosomes. Neuron, 21, 147-154.
    • (1998) Neuron , vol.21 , pp. 147-154
    • Tandon, A.1    Bannykh, S.2    Kowalchyk, J.A.3    Banerjee, A.4    Martin, T.F.5    Balch, W.E.6
  • 36
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L. Mimnaugh, E.G., De Costa, B., Myers, C.E. and Neckers, L.M. (1994) Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation. Proc. Natl Acad. Sci. USA, 91, 8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 37
    • 0030446448 scopus 로고    scopus 로고
    • Structural insights into the function of the Rab GDI superfamily
    • Wu, S.K., Zeng, K., Wilson, I.A. and Balch, W.E. (1996) Structural insights into the function of the Rab GDI superfamily. Trends Biochem. Sci., 21, 472-476.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 472-476
    • Wu, S.K.1    Zeng, K.2    Wilson, I.A.3    Balch, W.E.4
  • 38
    • 0032500665 scopus 로고    scopus 로고
    • Molecular role for the Rab binding platform of guanine nucleotide dissociation inhibitor in endoplasmic reticulum to Golgi transport
    • Wu, S.K., Luan, P., Matteson, J., Zeng, K., Nishimura, N. and Balch, W.E. (1998) Molecular role for the Rab binding platform of guanine nucleotide dissociation inhibitor in endoplasmic reticulum to Golgi transport. J. Biol. Chem., 273, 26931-26938.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26931-26938
    • Wu, S.K.1    Luan, P.2    Matteson, J.3    Zeng, K.4    Nishimura, N.5    Balch, W.E.6
  • 39
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young, J.C., Moarefi, I. and Hartl, F.U. (2001) Hsp90: A specialized but essential protein-folding tool. J. Cell Biol., 154, 267-273.
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 40
  • 41
    • 0035400710 scopus 로고    scopus 로고
    • Molecular chaperones and the regulation of neurotransmitter exocytosis
    • Zinsmaier, K.E. and Bronk, P. (2001) Molecular chaperones and the regulation of neurotransmitter exocytosis. Biochem. Pharmacol., 62, 1-11.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 1-11
    • Zinsmaier, K.E.1    Bronk, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.