Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.

ABSTRACT: Cellular function is based on protein-protein interactions. A large proportion of these interactions involves the binding of short linear motifs (SLiMs) by folded globular domains. These interactions are regulated by post-translational modifications, such as phosphorylation, that create and break motif binding sites or tune the affinity of the interactions. In addition, motif-based interactions are involved in targeting serine/threonine kinases and phosphatases to their substrate and contribute to the specificity of the enzymatic actions regulating which sites are phosphorylated. Here, we review how SLiM-based interactions assist in determining the specificity of serine/threonine kinases and phosphatases, and how phosphorylation, in turn, affects motif-based interactions. We provide exampl

SUBMITTER: Kliche J 

PROVIDER: S-EPMC8786283 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature