Lysine Acetylation Reshapes the Downstream Signaling Landscape of Vav1 in Lymphocytes.

ABSTRACT: Vav1 works both as a catalytic Rho GTPase activator and an adaptor molecule. These functions, which are critical for T cell development and antigenic responses, are tyrosine phosphorylation-dependent. However, it is not known whether other posttranslational modifications can contribute to the regulation of the biological activity of this protein. Here, we show that Vav1 becomes acetylated on lysine residues in a stimulation- and SH2 domain-dependent manner. Using a collection of both acetylation- and deacetylation-mimicking mutants, we show that the acetylation of four lysine residues (Lys²²², Lys²⁵², Lys⁵⁸⁷, and Lys⁷¹⁶) leads to the downmodulation of the adaptor function of Vav1 that triggers the stimulation of the nuclear factor of activated T

SUBMITTER: Rodriguez-Fdez S 

PROVIDER: S-EPMC7140538 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature