Nakamura N, Lowe M, Levine T P, Rabouille C, Warren G
Cell Biology Laboratory, Imperial Cancer Research Fund, London, United Kingdom.
Cell. 1997 May 2;89(3):445-55. doi: 10.1016/s0092-8674(00)80225-1.
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.
运输小泡与靶膜的对接被认为是由p115介导的。我们在此表明，顺式高尔基体基质蛋白GM130与p115特异性相互作用，因此可能提供一个膜对接位点。缺失分析表明，N端与p115结合，而C端与高尔基体膜结合。GM130或其N端衍生肽的有丝分裂磷酸化阻止了与p115的结合。该肽还抑制了有丝分裂片段中高尔基体潴泡的NSF依赖性但非p97依赖性重新组装，除非它被有丝分裂磷酸化。总之，这些数据为有丝分裂开始时COPI介导的高尔基体断裂提供了分子解释。
