Clathrin recruits PIK3C2A

Stable Identifier
Reaction [binding]
Homo sapiens
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PIK3C2A is a member of the class II PI 3 kinases, and phosphorylates PI(4)P to PI(3,4)P2 at the plasma membrane. PIK3C2A interacts with clathrin through a clathrin-binding domain in its unique N-terminal tail and localizes to late-stage clathrin-coated pits (Domin et al, 2000; Gaidarov et al, 2001; Gaidarov et al, 2005). Binding to clathrin stimulates the kinase activity of PIK3C2A and promotes the production of PI(3,4)P2 at the plasma membrane (Gaidarov et al, 2001). PI(3,4)P2 formation by PIK3C2A contributes to maturation of clathrin-coated pits by promoting the recruitment of BAR-domain containing proteins such as SNX9, which stimulate membrane curvature required for vesicle formation and eventual fission (Posor et al, 2013; reveiwed in Daumke et al, 2014).
Literature References
PubMed ID Title Journal Year
16215232 Individual phosphoinositide 3-kinase C2alpha domain activities independently regulate clathrin function

Gaidarov, I, Zhao, Y, Keen, JH

J. Biol. Chem. 2005
11239472 The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking

Domin, J, Gaidarov, I, Smith, ME, Keen, JH

Mol. Cell 2001
10766823 The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles

Waterfield, MD, Gaidarov, I, Domin, J, Smith, ME, Keen, JH

J Biol Chem 2000
24581490 BAR domain scaffolds in dynamin-mediated membrane fission

Daumke, O, Haucke, V, Roux, A

Cell 2014
23823722 Spatiotemporal control of endocytosis by phosphatidylinositol-3,4-bisphosphate

Haucke, V, Schultz, C, Hirsch, E, Schmoranzer, J, Gulluni, F, Puchkov, D, Noé, F, Posor, Y, Zarbakhsh, S, Eichhorn-Gruenig, M, Müller, R, Ullrich, A, Schöneberg, J, Lampe, A, Krauss, M

Nature 2013
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