Competitive Interactions between PIRT, the Cold Sensing Ion Channel TRPM8, and PIP₂ Suggest a Mechanism for Regulation.

ABSTRACT: TRPM8 is a member of the transient receptor potential ion channel family where it functions as a cold and pain sensor in humans and other higher organisms. Previous studies show that TRPM8 requires the signaling phosphoinositide lipid PIP₂ to function. TRPM8 function is further regulated by other diverse mechanisms, including the small modulatory membrane protein PIRT (phosphoinositide regulator of TRP). Like TRPM8, PIRT also binds PIP₂ and behavioral studies have shown that PIRT is required for normal TRPM8-mediated cold-sensing. To better understand the molecular mechanism of PIRT regulation of TRPM8, solution nuclear magnetic resonance (NMR) spectroscopy was used to assign the backbone resonances of full-length human PIRT and investigate the direct binding of PIRT

SUBMITTER: Sisco NJ 

PROVIDER: S-EPMC6773951 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature