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A more recent version of this article appeared on December 9, 2005
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Papers In Press, published online ahead of print October 7, 2005
J. Biol. Chem, 10.1074/jbc.M507731200
Submitted on July 15, 2005
Accepted on October 7, 2005

Individual Pl 3-kinase C2alpha domain activities independently regulate clathrin function

Ibragim Gaidarov, Yanqiu Zhao, and James H. Keen

Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107

Corresponding Author: jim.keen{at}mail.jci.tju.edu

Phosphoinositide 3-kinase C2a, (PI3K-C2a,) is a member of the class II PI-3 kinases, defined by the presence of a second C2 domain at their C-terminus. The cellular functions of the class II enzymes are incompletely understood, though they have been implicated in receptor activation pathways initiated by EGF, insulin and chemokines. PI3K-C2a, was recently found to be localized to clathrin coated membranes in the trans-Golgi network and at endocytic sites on the plasma membrane. Further, a specific binding site was identified for clathrin on the N-terminus of PI3K-C2a, whose occupancy resulted in lipid kinase activation. Expression of PI3K-C2a, in cells dramatically affected clathrin distribution and function in cells, leading to accumulation of intracellular clathrin coated structures, which are visualized here at the ultrastructural level, and inhibition of clathrin mediated transport from both the plasma membrane and TGN. In this study we demonstrate that the isolated clathrin binding domain of PI3K-C2a can drive clathrin lattice assembly, and that both it and the protein’s lipid kinase activity can independently modulate clathrin distribution and function when expressed in cells. Together, these results suggest that PI3K-C2a employs both protein-protein interaction and localized production of 3-phosphoinositides to affect clathrin dynamics at sites of membrane budding and targeting.


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