The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner

被引:345
作者
Nakamura, N [1 ]
Lowe, M [1 ]
Levine, TP [1 ]
Rabouille, C [1 ]
Warren, G [1 ]
机构
[1] IMPERIAL CANC RES FUND, CELL BIOL LAB, LONDON WC2A 3PX, ENGLAND
基金
英国惠康基金;
关键词
D O I
10.1016/S0092-8674(00)80225-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The docking of transport vesicles with their target membrane is thought to be mediated by p115. We show here that GM130, a cis-Golgi matrix protein, interacts specifically with p115 and so could provide a membrane docking site. Deletion analysis showed that the N-terminus binds to p115, whereas the C-terminus binds to Golgi membranes. Mitotic phosphorylation of GM130 or a peptide derived from the N-terminus prevented binding to p115. The peptide also inhibited the NSF- but not the p97-dependent reassembly of Golgi cisternae from mitotic fragments, unless it was mitotically phosphorylated. Together, these data provide a molecular explanation for the COPI-mediated fragmentation of the Golgi apparatus at the onset of mitosis.
引用
收藏
页码:445 / 455
页数:11
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