Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release
Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release
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DOI：
10.1038/ncb1665
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发表时间：
2008-01-01
影响因子：
21.3
通讯作者：
Hirokawa, Nobutaka
中科院分区：
文献类型：
--
作者：
Guillaud, Laurent;Wong, Richard;Hirokawa, Nobutaka
细胞结构和功能的建立和维持高度依赖于对细胞内转运的有效调控，其中驱动蛋白超家族（KIFs）的蛋白质是非常重要的。在这方面，KIF如何监管其货物的释放是一个关键过程，仍有待阐明。为了解决这个具体问题，我们研究了KIF 17-Mint 1相互作用调控背后的机制。在这里，我们报告的分子马达KIF 17的尾部区域是由磷酸化调节。通过FRET和各种体外和体内方法直接可视化蛋白质-蛋白质相互作用，我们已经证明，CaMKII依赖性磷酸化KIF 17对Ser 1029的破坏KIF 17-Mint 1协会，并导致从其基于微管的运输释放运输货物。
Establishment and maintenance of cell structures and functions are highly dependent on the efficient regulation of intracellular transport in which proteins of the kinesin superfamily ( KIFs) are very important. In this regard, how KIFs regulate the release of their cargo is a critical process that remains to be elucidated. To address this specific question, we have investigated the mechanism behind the regulation of the KIF17-Mint1 interaction. Here we report that the tail region of the molecular motor KIF17 is regulated by phosphorylation. Using direct visualization of protein-protein interaction by FRET and various in vitro and in vivo approaches we have demonstrated that CaMKII-dependent phosphorylation of KIF17 on Ser 1029 disrupts the KIF17-Mint1 association and results in the release of the transported cargo from its microtubule-based transport.