Korolchuk V, Banting G
Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK.
Biochem Soc Trans. 2003 Aug;31(Pt 4):857-60. doi: 10.1042/bst0310857.
The process of clathrin-coated vesicle (CCV) formation/disassembly has been studied intensively, and numerous proteins have been identified which aid this process. We have learnt a great deal about individual components of the CCV machinery, and now the ultimate aim is to elucidate the mechanisms regulating clathrin-mediated trafficking. One of the fundamental processes governing the complicated network of interactions is phosphorylation. It has been known for some time that several proteins associated with clathrin-coated vesicles are substrates for protein kinases. These proteins include clathrin, three of the four adaptor complex subunits, dynamin 1, synaptojanin 1 and the amphiphysins. However, the identities of the kinases involved in this process remained largely unknown until recently. This short review discusses advances in our knowledge of how CCV formation/disassembly is regulated by the phosphorylation/dephosphorylation cycle and the role played by specific protein kinases in that process.
网格蛋白包被小泡(CCV)的形成/解体过程已得到深入研究,并且已鉴定出许多有助于此过程的蛋白质。我们已经对CCV机制的各个组成部分有了很多了解,现在的最终目标是阐明调节网格蛋白介导的运输的机制。控制复杂相互作用网络的基本过程之一是磷酸化。一段时间以来,人们已经知道几种与网格蛋白包被小泡相关的蛋白质是蛋白激酶的底物。这些蛋白质包括网格蛋白、四种衔接蛋白复合体亚基中的三种、发动蛋白1、突触素1和双栖蛋白。然而,直到最近,参与这一过程的激酶的身份在很大程度上仍不清楚。这篇简短的综述讨论了我们在CCV形成/解体如何受磷酸化/去磷酸化循环调节以及特定蛋白激酶在该过程中所起作用方面的知识进展。