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J Biol Chem. 2005 Jun 3;280(22):21539-44. Epub 2005 Apr 4.

CVAK104 is a novel poly-L-lysine-stimulated kinase that targets the beta2-subunit of AP2.

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  • 1Department of Genetics, Cell Biology, and Development, The University of Minnesota, Minneapolis, Minnesota 55455, USA. sdconner@umn.edu


Isolated clathrin adaptor protein (AP) preparations are known to co-fractionate with endogenous kinase activities, including poly-L-lysine-stimulated kinases that target various constituents of the clathrin coat. We have identified CVAK104 (a coated vesicle-associated kinase of 104 kDa) using a mass spectroscopic analysis of adaptor protein preparations. CVAK104 is a novel serine/threonine kinase that belongs to the SCY1-like family of protein kinases, previously thought to be catalytically inactive. We found that CVAK104 co-fractionates with adaptor protein preparations extracted from clathrin-coated vesicles and directly binds to both clathrin and the plasma membrane adaptor, AP2. CVAK104 binds ATP, and kinase assays indicate that it functions in vitro as a poly-L-lysine-stimulated kinase that is capable of autophosphorylation and phosphorylating the beta2-adaptin subunit of AP2.

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