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A phosphatidylinositol (4,5)-bisphosphate binding site within mu 2-adaptin regulates clathrin-mediated endocytosis

MPG-Autoren
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Wenzel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Zitation

Rohde, G., Wenzel, D., & Haucke, V. (2002). A phosphatidylinositol (4,5)-bisphosphate binding site within mu 2-adaptin regulates clathrin-mediated endocytosis. Journal of Cell Biology, 158(2), 209-214. Retrieved from http://jcb.rupress.org/content/158/2/209.full.pdf+html.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0012-F36D-B
Zusammenfassung
The clathrin adaptor complex AP-2 serves to coordinate clathrin-coated pit assembly with the sorting of transmembrane cargo proteins at the plasmalemma. Flow precisely AP-2 assembly and cargo protein recognition at sites of endocytosis are regulated has remained unclear, but recent evidence implicates phosphoinositides, in particular phosphatidylinositol (4,5)- bisphosphate (PI[4,5]P-2) in these processes. Here we have identified and functionally characterized a conserved binding site for PI(4,5)P2 within mu2-adaptin, the medium chain of the clathrin adaptor complex AP-2. Mutant p,2 lacking a cluster of conserved lysine residues fails to bind PI(4,5)P2 and to compete the recruitment of native clathrin/AP-2 to PI(4,5)P-2- containing liposomes or to presynaptic membranes. Moreover, we show that expression of mutant mu2 inhibits receptor-mediated endocytosis in living cells. We suggest that PI(4,5)P-2 binding to mu2-adaptin regulates clathrin-mediated endocytosis and thereby may contribute to structurally linking cargo recognition to coat formation.