메뉴 건너뛰기




Volumn 8, Issue 3, 2007, Pages 236-240

Calcium: A fundamental regulator of intracellular membrane fusion?

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM;

EID: 33847388051     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400921     Document Type: Review
Times cited : (133)

References (29)
  • 1
    • 0025947123 scopus 로고
    • Alien intracellular calcium chelators attenuate neurotransmitter release at the squid giant synapse
    • Adler EM, Augustine GJ, Duffy SN, Charlton MP (1991) Alien intracellular calcium chelators attenuate neurotransmitter release at the squid giant synapse. J Neurosci 11: 1496-1507
    • (1991) J Neurosci , vol.11 , pp. 1496-1507
    • Adler, E.M.1    Augustine, G.J.2    Duffy, S.N.3    Charlton, M.P.4
  • 3
    • 0024596794 scopus 로고
    • Calcium and GTP: Essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus
    • Beckers CJ, Balch WE (1989) Calcium and GTP: Essential components in vesicular trafficking between the endoplasmic reticulum and Golgi apparatus. J Cell Biol 108: 1245-1256
    • (1989) J Cell Biol , vol.108 , pp. 1245-1256
    • Beckers, C.J.1    Balch, W.E.2
  • 4
    • 0042160096 scopus 로고    scopus 로고
    • Calcium and calmodulin in membrane fusion
    • Burgoyne RD, Clague MJ (2003) Calcium and calmodulin in membrane fusion. Biochim Biophys Acta 1641: 137-143
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 137-143
    • Burgoyne, R.D.1    Clague, M.J.2
  • 6
    • 0036878788 scopus 로고    scopus 로고
    • Calcium leak from intracellular stores: The enigma of calcium signalling
    • Camello C, Lomax R, Petersen OH, Tepikin AV (2002) Calcium leak from intracellular stores: The enigma of calcium signalling. Cell Calcium 32: 355-361
    • (2002) Cell Calcium , vol.32 , pp. 355-361
    • Camello, C.1    Lomax, R.2    Petersen, O.H.3    Tepikin, A.V.4
  • 7
    • 0037144587 scopus 로고    scopus 로고
    • Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell
    • Chen JL, Ahluwalia JP, Stamnes M (2002) Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell. J Biol Chem 277: 35682-35687
    • (2002) J Biol Chem , vol.277 , pp. 35682-35687
    • Chen, J.L.1    Ahluwalia, J.P.2    Stamnes, M.3
  • 8
    • 0030944210 scopus 로고    scopus 로고
    • Calmodulin regulates endosome fusion
    • Colombo MI, Beron W, Stahl PD (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
  • 9
    • 0344875996 scopus 로고    scopus 로고
    • Calmodulin-dependent regulation of a lipid binding domain in the v-SNARE synaptobrevin and its role in vesicular fusion
    • De Haro L, Quetglas S, Iborra C, Leveque C, Seagar M (2003) Calmodulin-dependent regulation of a lipid binding domain in the v-SNARE synaptobrevin and its role in vesicular fusion. Biol Cell 95: 459-464
    • (2003) Biol Cell , vol.95 , pp. 459-464
    • De Haro, L.1    Quetglas, S.2    Iborra, C.3    Leveque, C.4    Seagar, M.5
  • 10
    • 33644857375 scopus 로고    scopus 로고
    • Cysteine-disulfide cross-linking to monitor SNARE complex assembly during endoplasmic reticulum-Golgi transport
    • Flanagan JJ, Barlowe C (2006) Cysteine-disulfide cross-linking to monitor SNARE complex assembly during endoplasmic reticulum-Golgi transport. J Biol Chem 281: 2281-2288
    • (2006) J Biol Chem , vol.281 , pp. 2281-2288
    • Flanagan, J.J.1    Barlowe, C.2
  • 11
    • 14044278863 scopus 로고    scopus 로고
    • Interaction of neuronal calcium sensor-1 and ADP-ribosylation factor 1 allows bidirectional control of phosphatidylinositol 4-kinase β and trans-Golgi network-plasma membrane traffic
    • Haynes LP, Thomas GM, Burgoyne RD (2005) Interaction of neuronal calcium sensor-1 and ADP-ribosylation factor 1 allows bidirectional control of phosphatidylinositol 4-kinase β and trans-Golgi network-plasma membrane traffic. J Biol Chem 280: 6047-6054
    • (2005) J Biol Chem , vol.280 , pp. 6047-6054
    • Haynes, L.P.1    Thomas, G.M.2    Burgoyne, R.D.3
  • 12
    • 0032824099 scopus 로고    scopus 로고
    • Fusion of endosomes involved in synaptic vesicle recycling
    • Holroyd C, Kistner U, Annaert W, 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
  • 13
    • 16244412642 scopus 로고    scopus 로고
    • Masters or slaves? Vesicle release machinery and the regulation of presynaptic calcium channels
    • Jarvis SE, Zamponi GW (2005) Masters or slaves? Vesicle release machinery and the regulation of presynaptic calcium channels. Cell Calcium 37: 483-488
    • (2005) Cell Calcium , vol.37 , pp. 483-488
    • Jarvis, S.E.1    Zamponi, G.W.2
  • 14
    • 1642539980 scopus 로고    scopus 로고
    • 2+ efflux from the yeast vacuole lumen
    • 2+ efflux from the yeast vacuole lumen. J Cell Biol 164: 195-206
    • (2004) J Cell Biol , vol.164 , pp. 195-206
    • Merz, A.J.1    Wickner, W.T.2
  • 15
    • 0034988109 scopus 로고    scopus 로고
    • Relationships between EEA1 binding partners and their role in endosome fusion
    • Mills IG, Urbe S, Clague MJ (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
  • 16
    • 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
  • 17
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozenfreeze dried PC12 cells
    • Pezzati R, Bossi M, Podini P, Meldolesi J, Grohovaz F (1997) High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Electron energy loss imaging analysis of quick frozenfreeze dried PC12 cells. Mol Biol Cell 8: 1501-1512
    • (1997) Mol Biol Cell , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 18
    • 0034703092 scopus 로고    scopus 로고
    • Regulation of intra-Golgi membrane transport by calcium
    • Porat A, Elazar Z (2000) Regulation of intra-Golgi membrane transport by calcium. J Biol Chem 275: 29233-29237
    • (2000) J Biol Chem , vol.275 , pp. 29233-29237
    • Porat, A.1    Elazar, Z.2
  • 19
    • 0034729167 scopus 로고    scopus 로고
    • 2+ in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • 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
  • 20
    • 20444476585 scopus 로고    scopus 로고
    • Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae
    • Starai VJ, Thorngren N, Fratti RA, Wickner W (2005) Ion regulation of homotypic vacuole fusion in Saccharomyces cerevisiae. J Biol Chem 280: 16754-16762
    • (2005) J Biol Chem , vol.280 , pp. 16754-16762
    • Starai, V.J.1    Thorngren, N.2    Fratti, R.A.3    Wickner, W.4
  • 21
    • 0038825173 scopus 로고    scopus 로고
    • Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
    • Sun W, Yan Q, Vida TA, Bean AJ (2003) Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex. J Cell Biol 162: 125-137
    • (2003) J Cell Biol , vol.162 , pp. 125-137
    • Sun, W.1    Yan, Q.2    Vida, T.A.3    Bean, A.J.4
  • 22
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang J, Maximov A, Shin OH, Dai H, Rizo J, Sudhof TC (2006) A complexin/ synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126: 1175-1187
    • (2006) Cell , vol.126 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.H.3    Dai, H.4    Rizo, J.5    Sudhof, T.C.6
  • 25
    • 11244273061 scopus 로고    scopus 로고
    • Reconstitution of COPII vesicle fusion to generate a pre- Golgi intermediate compartment
    • Xu D, Hay JC (2004) Reconstitution of COPII vesicle fusion to generate a pre- Golgi intermediate compartment. J Cell Biol 167: 997-1003
    • (2004) J Cell Biol , vol.167 , pp. 997-1003
    • Xu, D.1    Hay, J.C.2
  • 26
    • 33750534358 scopus 로고    scopus 로고
    • The Ca-binding protein ALG-2 is recruited to ER exit sites by sec31A and stabilizes the localization of sec31A
    • Yamasaki A, Komada M (2006) The Ca-binding protein ALG-2 is recruited to ER exit sites by sec31A and stabilizes the localization of sec31A. Mol Biol Cell 17: 4876-4887
    • (2006) Mol Biol Cell , vol.17 , pp. 4876-4887
    • Yamasaki, A.1    Komada, M.2
  • 27
    • 2442492169 scopus 로고    scopus 로고
    • 2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes
    • 2+ and N-ethylmaleimide-sensitive factor differentially regulate disassembly of SNARE complexes on early endosomes. J Biol Chem 279: 18270-18276
    • (2004) J Biol Chem , vol.279 , pp. 18270-18276
    • Yan, Q.1    Sun, W.2    McNew, J.A.3    Vida, T.A.4    Bean, A.J.5
  • 29
    • 33745480157 scopus 로고    scopus 로고
    • Ryanodine receptor interaction with the SNARE-associated protein snapin
    • Zissimopoulos S, West DJ, Williams AJ, Lai FA (2006) Ryanodine receptor interaction with the SNARE-associated protein snapin. J Cell Sci 119: 2386-2397
    • (2006) J Cell Sci , vol.119 , pp. 2386-2397
    • Zissimopoulos, S.1    West, D.J.2    Williams, A.J.3    Lai, F.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.