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• W2121036696 startingPage "3153" @default.
• W2121036696 abstract "The Wiskott-Aldrich syndrome protein (WASp) is a key regulator of actin dynamics during cell motility and adhesion, and mutations in its gene are responsible for Wiskott-Aldrich syndrome (WAS). Here, we demonstrate that WASp is ubiquitylated following T-cell antigen receptor (TCR) activation. WASp phosphorylation at tyrosine 291 results in recruitment of the E3 ligase Cbl-b, which, together with c-Cbl, carries out WASp ubiquitylation. Lysine residues 76 and 81, located at the WASp WH1 domain, which contains the vast majority of WASp gene mutations, serve as the ubiquitylation sites. Disruption of WASp ubiquitylation causes WASp accumulation and alters actin dynamics and the formation of actin-dependent structures. Our data suggest that regulated degradation of activated WASp might be an efficient strategy by which the duration and localization of actin rearrangement and the intensity of T-cell activation are controlled." @default.
• W2121036696 created "2016-06-24" @default.
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• W2121036696 date "2012-08-01" @default.
• W2121036696 modified "2023-10-12" @default.
• W2121036696 title "Ubiquitylation-Dependent Negative Regulation of WASp Is Essential for Actin Cytoskeleton Dynamics" @default.
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• W2121036696 doi "https://doi.org/10.1128/mcb.00161-12" @default.
• W2121036696 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3434509" @default.
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• W2121036696 hasPublicationYear "2012" @default.
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