Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis

Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
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DOI:
10.1016/s0092-8674(00)81737-7
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发表时间:
1998-09-18
期刊:
影响因子:
64.5
通讯作者:
Warren, G
Warren, G
中科院分区:
生物学1区
文献类型:
--
作者:
Lowe, M;Rabouille, C;Warren, G

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高尔基体的有丝分裂可以很大程度上解释为破坏GM 130和囊泡对接蛋白p115之间的相互作用。在这里,我们确定了一个单一的丝氨酸(Ser-25)在GM 130作为关键的磷酸化目标和Cdc 2作为负责激酶。MEK 1,最近牵连在有丝分裂高尔基体片段的MAP激酶信号通路的一个组成部分,不需要GM 130磷酸化或有丝分裂片段在体外或体内。我们建议,Cdc 2直接参与有丝分裂高尔基体片段化,并通过MEK 1信号是不需要这个过程。
Mitotic fragmentation of the Golgi apparatus can be largely explained by disruption of the interaction between GM130 and the vesicle-docking protein p115. Here we identify a single serine (Ser-25) in GM130 as the key phosphorylated target and Cdc2 as the responsible kinase. MEK1, a component of the MAP kinase signaling pathway recently implicated in mitotic Golgi fragmentation, was not required for GM130 phosphorylation or mitotic fragmentation either in vitro or in vivo. We propose that Cdc2 is directly involved in mitotic Golgi fragmentation and that signaling via MEK1 is not required for this process.