P90RSK2, a new MLCK mediates contractility in myosin light chain kinase null smooth muscle.

ABSTRACT: Introduction: Phosphorylation of smooth muscle (SM) myosin regulatory light chain (RLC₂₀) is a critical switch leading to SM contraction. The canonical view held that only the short isoform of myosin light chain kinase (MLCK1) catalyzed this reaction. It is now accepted that auxiliary kinases may contribute to vascular SM tone and contractility. We have previously reported that p90 ribosomal S6 kinase (RSK2) functions as such a kinase, in parallel with MLCK1, contributing ∼25% of the maximal myogenic force in resistance arteries. Thus, RSK2 may be instrumental in the regulation of basal vascular tone and blood pressure. Here, we take advantage of a MLCK1 null mouse (mylk1 ^-/-) to further test our hypothesis that RSK2 can function as an MLCK, playing a si

SUBMITTER: Kalra J 

PROVIDER: S-EPMC10533999 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature