Kinases in clathrin-mediated endocytosis. (1st August 2003)

• Record Type: Journal Article
• Authors: Korolchuk, V.; Banting, G.
• Is Part Of: Biochemical Society transactions. Volume 31:Number 4(2003)
• Page Start: 857
• Page End: 860
• Publication Date: 2003-08-01
• Subjects: adaptor protein-2 (AP-2) -- clathrin-coated vesicle -- clathrin-mediated endocytosis -- kinase -- phosphorylation; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0310857
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : 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.