التفاصيل البيبلوغرافية
| العنوان: |
Pak1 Phosphorylation Enhances Cortactin–N-WASP Interaction in Clathrin-Caveolin-Independent Endocytosis. |
| المؤلفون: |
Grassart, Alexandre, Meas-Yedid, Vannary, Dufour, Alexandre, Olivo-Marin, Jean-Christophe, Dautry-Varsat, Alice, Sauvonnet, Nathalie |
| المصدر: |
Traffic; Aug2010, Vol. 11 Issue 8, p1079-1091, 13p, 4 Color Photographs, 3 Black and White Photographs, 1 Diagram |
| مصطلحات موضوعية: |
PROTEIN kinases, PHOSPHORYLATION, CHEMICAL reactions, ENDOCYTOSIS, POLYMERIZATION, ACTIN |
| مستخلص: |
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-2Rβ 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-2Rβ 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-2Rβ 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. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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