Abstract
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.
Highlights
Endocytosis involves the invagination of specialized regions of the plasma membrane, which pinch off to form cargo-containing vesicles that are transported into the cell
We found that CVAK104 co-fractionates with adaptor protein preparations extracted from clathrincoated vesicles and directly binds to both clathrin and the plasma membrane adaptor, AP2
CVAK104 Isolation and Cloning—Isolated adaptor protein preparations co-fractionate with endogenous kinase activities that target various subunits of the AP2 complex
Summary
Endocytosis involves the invagination of specialized regions of the plasma membrane, which pinch off to form cargo-containing vesicles that are transported into the cell. 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.
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