Phosphorylation of distal C-terminal residues promotes TRPV4 channel activation in response to arachidonic acid.

ABSTRACT: Transient receptor potential vanilloid 4 (TRPV4) is a Ca²⁺-permeable channel activated by diverse physical and chemical stimuli, including mechanical stress and endogenous lipid arachidonic acid (AA) and its metabolites. Phosphorylation of TRPV4 by protein kinase A (PKA) and protein kinase C (PKC) is a predominant mechanism for channel regulation, especially in the cytoplasmic domains due to their importance in protein assembly, and channelopathies. However, studies corresponding to phosphorylation sites for these kinases remain incomplete. We investigated the role of Ser-823 residue as a potential phosphorylation site in regulating TRPV4 activity and chemical agonist-induced channel activation. Using mass spectrometry, we identified a new phosphorylation site Ser-823 residue an

SUBMITTER: Parthasarathy A 

PROVIDER: S-EPMC11903807 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature