Condensed-phase signaling can expand kinase specificity and respond to macromolecular crowding.

ABSTRACT: Phase separation can concentrate biomolecules and accelerate reactions. However, the mechanisms and principles connecting this mesoscale organization to signaling dynamics are difficult to dissect because of the pleiotropic effects associated with disrupting endogenous condensates. To address this limitation, we engineered new phosphorylation reactions within synthetic condensates. We generally found increased activity and broadened kinase specificity. Phosphorylation dynamics within condensates were rapid and could drive cell-cycle-dependent localization changes. High client concentration within condensates was important but not the main factor for efficient phosphorylation. Rather, the availability of many excess client-binding sites together with a flexible scaffold was crucial. Phospho

SUBMITTER: Sang D 

PROVIDER: S-EPMC10101210 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature