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Pak1 Phosphorylation Enhances Cortactin-N-WASP Interaction in Clathrin-Caveolin-Independent Endocytosis.

Abstract : Growing evidence indicates that kinases are central to the regulation of endocytic pathways. Previously, we identified p21-activated kinase 1 (Pak1) as the first specific regulator of clathrin- and caveolae-independent endocytosis used by the interleukin 2 receptor subunit (IL-2R). Here, we address the mechanism by which Pak1 regulates IL-2Rbeta endocytosis. First, we show that Pak1 phosphorylates an activator of actin polymerization, cortactin, on its serine residues 405 and 418. Consistently, we observe a specific inhibition of IL-2Rbeta endocytosis when cells overexpress a cortactin, wherein these serine residues have been mutated. In addition, we show that the actin polymerization enhancer, neuronal Wiskott-Aldrich syndrome protein (N-WASP), is involved in IL-2Rbeta endocytosis. Strikingly, we find that Pak1 phosphorylation of cortactin on serine residues 405 and 418 increases its association with N-WASP. Thus, Pak1, by controlling the interaction between cortactin and N-WASP, could regulate the polymerization of actin during clathrin-independent endocytosis.
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Contributor : Marie Lemesle Connect in order to contact the contributor
Submitted on : Thursday, July 15, 2010 - 1:16:53 PM
Last modification on : Thursday, April 7, 2022 - 10:10:30 AM
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Alexandre Grassart, Vannary Meas-Yedid, Alexandre Dufour, Jean-Christophe Olivo-Marin, Alice Dautry-Varsat, et al.. Pak1 Phosphorylation Enhances Cortactin-N-WASP Interaction in Clathrin-Caveolin-Independent Endocytosis.. Traffic, Wiley, 2010, 11 (8), pp.1079-91. ⟨10.1111/j.1600-0854.2010.01075.x⟩. ⟨pasteur-00502612⟩



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