RLIP, an effector of the Ral GTPases, is a platform for cdk1 to phosphorylate Epsin during the switch off of endocytosis in mitosis
RLIP, an effector of the Ral GTPases, is a platform for cdk1 to phosphorylate Epsin during the switch off of endocytosis in mitosis
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DOI：
10.1074/jbc.m302191200
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发表时间：
2003-08-15
影响因子：
4.8
通讯作者：
Camonis, J
中科院分区：
文献类型：
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作者：
Rossé, C;L'Hoste, B;Camonis, J
RAL信号通路在RAS依赖的肿瘤发生中起重要作用。RLIP/RalBP1是其关键分子之一，它在间期参与受体的内吞作用，当内吞作用被关闭时也参与有丝分裂过程。在有丝分裂过程中，RLIP76位于复制的中心体上，是中心体正确分离和运动到两极所必需的。我们一直在寻找在有丝分裂期间与RLIP相关的演员。我们在这里证明了RLIP/RalBP1与一个活性的p34cdc2.cyclinB1(CDK1)酶相互作用，这种相互作用对Epsin的有丝分裂磷酸化至关重要，一旦磷酸化，就不再具有内吞作用。我们还表明，后一种磷酸化依赖于Ral信号。我们认为RLIP/RalBP1是有丝分裂的CDK1利用RLIP/RalBP1作为平台来促进Epsin的磷酸化，当内吞作用被关闭时，Epsin在有丝分裂过程中不能进行内吞作用。
The Ral signaling pathway is critically involved in Ras-dependent oncogenesis. One of its key actors, RLIP/RalBP1, which participates in receptor endocytosis during interphase, is also involved in mitotic processes when endocytosis is switched off. During mitosis, RLIP76 is located on the duplicated centrosomes and is required for their proper separation and movement to the poles. We have looked for actors that associate with RLIP during mitosis. We show here that RLIP/RalBP1 interacts with an active p34cdc2.cyclinB1 (cdk1) enzyme and that this interaction is crucial for the mitotic phosphorylation of Epsin that, once phosphorylated, is no longer competent for endocytosis. We show also that this latter phosphorylation is dependent on Ral signaling. We propose that RLIP/RalBP1 is used as a platform by the mitotic cdk1 to facilitate the phosphorylation of Epsin, which makes Epsin incompetent for endocytosis during mitosis, when endocytosis is switched off.