메뉴 건너뛰기




Volumn 18, Issue 21, 1999, Pages 5885-5891

Disruption of Rab3-calmodulin interaction, but not other effector interactions, prevents Rab3 inhibition of exocytosis

Author keywords

GTP; Insulin; Neurotransmitter; Secretion

Indexed keywords

ARGININE; CALCIUM ION; CALMODULIN; GUANOSINE TRIPHOSPHATASE; NEUROTRANSMITTER; RAB PROTEIN;

EID: 0033230605     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.21.5885     Document Type: Article
Times cited : (84)

References (45)
  • 1
    • 0030705160 scopus 로고    scopus 로고
    • The stimulatory effect of rabphilin-3a on regulated exocytosis from insulin-secreting cells does not require an association-dissociation cycle with membranes mediated by Rab3
    • Arribas, M., Regazzi, R., Garcia, E., Wollheim, C.B. and De Camilli, P. (1997) The stimulatory effect of rabphilin-3a on regulated exocytosis from insulin-secreting cells does not require an association-dissociation cycle with membranes mediated by Rab3. Eur. J. Cell Biol., 74, 209-216.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 209-216
    • Arribas, M.1    Regazzi, R.2    Garcia, E.3    Wollheim, C.B.4    De Camilli, P.5
  • 2
    • 0030786774 scopus 로고    scopus 로고
    • Better late than never: A role for Rabs late in exocytosis
    • Bean, A.J. and Scheller, R.H. (1997) Better late than never: a role for Rabs late in exocytosis. Neuron, 19, 751-754.
    • (1997) Neuron , vol.19 , pp. 751-754
    • Bean, A.J.1    Scheller, R.H.2
  • 4
    • 0027519409 scopus 로고
    • Regulation of the GTPase cycle of the neuronally expressed Raslike GTP-binding protein Rab3A
    • Burstein, E.S., Brondyk, W.H., Macara, I.A., Kaibuchi, K. and Takai, Y. (1993) Regulation of the GTPase cycle of the neuronally expressed Raslike GTP-binding protein Rab3A. J. Biol. Chem., 268, 22247-22250.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22247-22250
    • Burstein, E.S.1    Brondyk, W.H.2    Macara, I.A.3    Kaibuchi, K.4    Takai, Y.5
  • 5
    • 0028149342 scopus 로고
    • Specific interactions of Mss4 with members of the Rab GTPase subfamily
    • Burton, J.L., Burns, M.E., Gatti, E., Augustine, G.J. and De Camilli, P. (1994) Specific interactions of Mss4 with members of the Rab GTPase subfamily. EMBO J., 13, 5547-5558.
    • (1994) EMBO J. , vol.13 , pp. 5547-5558
    • Burton, J.L.1    Burns, M.E.2    Gatti, E.3    Augustine, G.J.4    De Camilli, P.5
  • 6
    • 0028978947 scopus 로고
    • Distinct effects of α-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 α-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
  • 7
    • 0029077932 scopus 로고
    • Evidence that the Rab3a-binding protein, Rabphilin-3a, enhances regulated secretion. Studies in adrenal chromaffin cells
    • Chung, S.-H., Takai, Y. and Holz, R.W. (1995) Evidence that the Rab3a-binding protein, Rabphilin-3a, enhances regulated secretion. Studies in adrenal chromaffin cells. J. Biol. Chem., 270, 16714-16718.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16714-16718
    • Chung, S.-H.1    Takai, Y.2    Holz, R.W.3
  • 8
    • 0033581022 scopus 로고    scopus 로고
    • Comparison of the effects on secretion in chromaffin and PC12 cells of Rab3 family members and mutants
    • Chung, S.-H., Joberty, G., Gelino, E.A., Macara, I.G. and Holz, R.W. (1999) Comparison of the effects on secretion in chromaffin and PC12 cells of Rab3 family members and mutants. J. Biol. Chem., 274, 18113-18120.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18113-18120
    • Chung, S.-H.1    Joberty, G.2    Gelino, E.A.3    Macara, I.G.4    Holz, R.W.5
  • 9
    • 0025830577 scopus 로고
    • C-terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester
    • Farnsworth, C.C., Kawata, M., Yoshida, Y., Takai, Y., Gelb, M.H. and Glomset, J.A. (1991) C-terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester. Proc. Natl Acad. Sci. USA, 88, 6196-6200.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6196-6200
    • Farnsworth, C.C.1    Kawata, M.2    Yoshida, Y.3    Takai, Y.4    Gelb, M.H.5    Glomset, J.A.6
  • 10
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick, S. and Jahn, R. (1994) Vesicle fusion from yeast to man. Nature, 370, 191-193.
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 11
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion
    • Geppert, M., Goda, Y., Stevens, C.F. and Südhof, T.C. (1997) The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. Nature, 387, 810-814.
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1    Goda, Y.2    Stevens, C.F.3    Südhof, T.C.4
  • 12
    • 0031898897 scopus 로고    scopus 로고
    • Rab3 and synaptotagmin: The yin and yang of synaptic membrane fusion
    • Geppert, M. and Südhof, 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    Südhof, T.C.2
  • 13
    • 0029922172 scopus 로고    scopus 로고
    • Evidence for a role of calmodulin in calcium-induced noradrenaline release from permeated synaptosomes: Effects of calmodulin antibodies and antagonists
    • Hens, J.J., Oestreicher, A.B., De Wit, M., Marquart, A., Gispen, W.H. and de Graan, P.N. (1996) Evidence for a role of calmodulin in calcium-induced noradrenaline release from permeated synaptosomes: effects of calmodulin antibodies and antagonists. J. Neurochem., 66, 1933-42.
    • (1996) J. Neurochem. , vol.66 , pp. 1933-1942
    • Hens, J.J.1    Oestreicher, A.B.2    De Wit, M.3    Marquart, A.4    Gispen, W.H.5    De Graan, P.N.6
  • 16
    • 0028356773 scopus 로고
    • The GTPase Rab3a negatively controls calcium-dependent exocytosis in neuroendocrine cells
    • Johannes, L., Lledo, P.-M., Roa, M., Vincent, J.-D., Henry, J.-P. and Darchen, F. (1994) The GTPase Rab3a negatively controls calcium-dependent exocytosis in neuroendocrine cells. EMBO J., 13, 2029-2037.
    • (1994) EMBO J. , vol.13 , pp. 2029-2037
    • Johannes, L.1    Lledo, P.-M.2    Roa, M.3    Vincent, J.-D.4    Henry, J.-P.5    Darchen, F.6
  • 18
    • 0030664819 scopus 로고    scopus 로고
    • Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells
    • Kotake, K., Ozaki, N., Mizuta, M., Sekiya, S., Inagaki, N. and Seino, S. (1997) Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells. J. Biol. Chem., 272, 29407-29410.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29407-29410
    • Kotake, K.1    Ozaki, N.2    Mizuta, M.3    Sekiya, S.4    Inagaki, N.5    Seino, S.6
  • 21
    • 0029785081 scopus 로고    scopus 로고
    • Role of the Rab3A-binding domain in targeting of Rabphilin-3A to vesicle membranes of PC12 cells
    • McKiernan, C.J., Stabila, P.F. and Macara, I.G. (1996) Role of the Rab3A-binding domain in targeting of Rabphilin-3A to vesicle membranes of PC12 cells. Mol. Cell. Biol., 16, 4985-4995.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4985-4995
    • McKiernan, C.J.1    Stabila, P.F.2    Macara, I.G.3
  • 22
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P. and Zerial, M. (1997) The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol., 9, 496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 23
    • 0031973309 scopus 로고    scopus 로고
    • Involvement of Rabphilin3 in endocytosis through interaction with Rabahptin5
    • Ohya, T., Sasaki, T., Kato, M. and Takai, Y. (1998) Involvement of Rabphilin3 in endocytosis through interaction with Rabahptin5. J. Biol. Chem., 273, 613-617.
    • (1998) J. Biol. Chem. , vol.273 , pp. 613-617
    • Ohya, T.1    Sasaki, T.2    Kato, M.3    Takai, Y.4
  • 25
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of Rabphilin-3A
    • Ostermeier, C. and Brunger, A.T. (1999) Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of Rabphilin-3A. Cell, 96, 363-374.
    • (1999) Cell , vol.96 , pp. 363-374
    • Ostermeier, C.1    Brunger, A.T.2
  • 26
  • 29
    • 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
  • 30
    • 0029126327 scopus 로고
    • Rab GDP dissociation inhibitor: Putting Rab GTPases in the right place
    • Pfeffer, S.R., Dirac-Svejstrup, B.A. and Soldati, T. (1995) Rab GDP dissociation inhibitor: putting Rab GTPases in the right place. J. Biol. Chem., 270, 17057-17059.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17057-17059
    • Pfeffer, S.R.1    Dirac-Svejstrup, B.A.2    Soldati, T.3
  • 31
    • 0026713293 scopus 로고
    • The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins
    • Regazzi, R., Kikuchi, A., Takai, Y. and Wollheim, C.B. (1992) The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins. J. Biol. Chem., 267, 17512-17519.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17512-17519
    • Regazzi, R.1    Kikuchi, A.2    Takai, Y.3    Wollheim, C.B.4
  • 33
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads, A.R. and Friedberg, F. (1997) Sequence motifs for calmodulin recognition. FASEB J., 11, 331-340.
    • (1997) FASEB J. , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 34
    • 0032561201 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II
    • 2+/calmodulin-dependent protein kinase II. J. Biol. Chem., 273, 28424-28429.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28424-28429
    • Rich, R.C.1    Schulman, H.2
  • 35
    • 0028143698 scopus 로고
    • Mechanism of intracellularprotein transport
    • Rothman, J.D. (1994) Mechanism of intracellularprotein transport. Nature, 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.D.1
  • 37
    • 0021972439 scopus 로고
    • Selective packaging of human growth hormone into synaptic vesicles in a rat neuronal (PC12) cell line
    • Schweitzer, E.S. and Kelly, R.B. (1985) Selective packaging of human growth hormone into synaptic vesicles in a rat neuronal (PC12) cell line. J. Cell Biol., 101, 667-676.
    • (1985) J. Cell Biol. , vol.101 , pp. 667-676
    • Schweitzer, E.S.1    Kelly, R.B.2
  • 38
    • 0027461829 scopus 로고
    • Rabphilin-3A, a putative target protein for smg p25A/rab3Ap25 small GTP-binding protein related to synaptotagmin
    • Shirataki, H., Kaibuchi, K., Sakoda, T., Kishida, S., Yamaguchi, T., Wada, K., Miyzaki, M. and Takai, Y. (1993) Rabphilin-3A, a putative target protein for smg p25A/rab3Ap25 small GTP-binding protein related to synaptotagmin. Mol. Cell. Biol., 13, 2061-2068.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2061-2068
    • Shirataki, H.1    Kaibuchi, K.2    Sakoda, T.3    Kishida, S.4    Yamaguchi, T.5    Wada, K.6    Miyzaki, M.7    Takai, Y.8
  • 39
    • 0028594078 scopus 로고
    • Rabphilin-3A is associated with synaptic vesicles through a vesicle protein in a manner independent of Rab3A
    • Shirataki, H., Yamamoto, T., Hagi, S., Miura, H., Oishi, H., Jin-no, Y., Senbonmatsu, T. and Takai, Y. (1994) Rabphilin-3A is associated with synaptic vesicles through a vesicle protein in a manner independent of Rab3A. J. Biol. Chem., 269, 32717-32720.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32717-32720
    • Shirataki, H.1    Yamamoto, T.2    Hagi, S.3    Miura, H.4    Oishi, H.5    Jin-No, Y.6    Senbonmatsu, T.7    Takai, Y.8
  • 40
    • 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., Südhof, 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    Südhof, T.C.4    Jahn, R.5
  • 42
    • 0024445114 scopus 로고
    • Ultrastructural immunocytochemical localization of B-50/GAP43, a protein kinase C substrate, in isolated presynaptic nerve terminals and neuronal growth cones
    • Van Lookeren-Campagne, M., Oestreicher, A.B., Van Bergen en Henegouwen, P.M.P. and Gispen, W.H. (1989) Ultrastructural immunocytochemical localization of B-50/GAP43, a protein kinase C substrate, in isolated presynaptic nerve terminals and neuronal growth cones. J. Neurocyt., 18, 479-489.
    • (1989) J. Neurocyt. , vol.18 , pp. 479-489
    • Van Lookeren-Campagne, M.1    Oestreicher, A.B.2    Van Bergen En Henegouwen, P.M.P.3    Gispen, W.H.4
  • 43
    • 0031041373 scopus 로고    scopus 로고
    • Isolation of a GDP/GTP exchange protein specific for the Rab3 subfamily small G proteins
    • Wada, M., Nakanishi, H., Satoh, A., Hirano, H., Obaishi, H., Matsuura, Y. and Takai, Y. (1997) Isolation of a GDP/GTP exchange protein specific for the Rab3 subfamily small G proteins. J. Biol. Chem., 272, 3875-3878.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3875-3878
    • Wada, M.1    Nakanishi, H.2    Satoh, A.3    Hirano, H.4    Obaishi, H.5    Matsuura, Y.6    Takai, Y.7
  • 44
    • 0030877243 scopus 로고    scopus 로고
    • Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
    • Wang, Y., Okamoto, M., Schmitz, F, Hofmann, K. and Südhof, T.C. (1997) Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion. Nature, 388, 593-598.
    • (1997) Nature , vol.388 , pp. 593-598
    • Wang, Y.1    Okamoto, M.2    Schmitz, F.3    Hofmann, K.4    Südhof, T.C.5
  • 45
    • 0345465665 scopus 로고    scopus 로고
    • Calmodulin supports both inactivation and facilitation of L-type calcium channels
    • Zühlke, R.D., Pitt, G.S., Deisseroth, K., Tsien, R.W. and Reuter, H. (1999) Calmodulin supports both inactivation and facilitation of L-type calcium channels. Nature, 399, 159-162.
    • (1999) Nature , vol.399 , pp. 159-162
    • Zühlke, R.D.1    Pitt, G.S.2    Deisseroth, K.3    Tsien, R.W.4    Reuter, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.