VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo

被引:175
作者
Uchiyama, K
Jokitalo, E
Kano, F
Murata, M
Zhang, XD
Canas, B
Newman, R
Rabouille, C
Pappin, D
Freemont, P
Kondo, H
机构
[1] Univ Cambridge, Cambridge Inst Med Res, Cambridge CB2 2XY, England
[2] Univ Helsinki, Inst Biotechnol, FIN-00014 Helsinki, Finland
[3] Natl Inst Physiol Sci, Okazaki, Aichi 4448585, Japan
[4] Univ London Imperial Coll Sci Technol & Med, Ctr Struct Biol, London SW7 2AZ, England
[5] Univ London Imperial Coll Sci Technol & Med, London W12 0NN, England
[6] European Mol Biol Lab, European Bioinformat Inst, Cambridge CB10 1SD, England
[7] Univ Utrecht, Acad Ziekenhuis, Med Ctr, NL-3584 CX Utrecht, Netherlands
基金
英国惠康基金;
关键词
membrane fusion; p97; VCIP135; Golgi; ER;
D O I
10.1083/jcb.200208112
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
NSF and p97 are ATPases required for the heterotypic fusion of transport vesicles with their target membranes and the homotypic fusion of organelles. NSF uses ATP hydrolysis to dissociate NSF/SNAPS/SNARES complexes, separating the v- and t-SNARES, which are then primed for subsequent rounds of fusion. In contrast, p97 does not dissociate the p97/p47/SNARE complex even in the presence of ATP. Now we have identified a novel essential factor for p97/p47-mediated membrane fusion, named VCIP135 (valosin-containing protein [VCP] [p97]/p47 complex-interacting protein, p135), and show that it binds to the p97/p47/syntaxin5 complex and dissociates it via p97 catalyzed ATP hydrolysis. In living cells, VCIP735 and p47 are shown to function in Golgi and ER assembly.
引用
收藏
页码:855 / 866
页数:12
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