The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
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DOI：
10.1016/s0092-8674(00)80225-1
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发表时间：
1997-05-02
期刊：
影响因子：
64.5
通讯作者：
Warren, G
中科院分区：
文献类型：
--
作者：
Nakamura, N;Lowe, M;Warren, G
转运囊泡与其靶膜的对接被认为是由p115介导的。我们在这里展示了GM130，一种顺式高尔基体基质蛋白，与p115特异地相互作用，因此可以提供一个膜对接位置。缺失分析表明，N端与p115结合，而C端与高尔基膜结合。GM130的有丝分裂磷酸化或来自N末端的多肽阻止了与p115的结合。该肽还抑制NSF，但不抑制依赖于p97的高尔基池有丝分裂片段的重组，除非它是有丝分裂磷酸化的。总之，这些数据为COPI介导的高尔基体在有丝分裂开始时的碎裂提供了分子解释。
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.