Phosphorylation regulates the sensitivity of voltage-gated Kv7.2 channels towards phosphatidylinositol-4,5-bisphosphate.

ABSTRACT:

Key points

Phosphatidylinositol-4,5-bisphosphate (PIP₂ ) is a key regulator of many membrane proteins, including voltage-gated Kv7.2 channels. In this study, we identified the residues in five phosphorylation sites and their corresponding protein kinases, the former being clustered within one of four putative PIP₂ -binding domains in Kv7.2. Dephosphorylation of these residues reduced the sensitivity of Kv7.2 channels towards PIP₂ . Dephosphorylation of Kv7.2 affected channel inhibition via M₁ muscarinic receptors, but not via bradykinin receptors. Our data indicated that phosphorylation of the Kv7.2 channel was necessary to maintain its low affinity for PIP₂ , thereby ensuring the tight regulation of the channel via G protein-c

SUBMITTER: Salzer I 

PROVIDER: S-EPMC5215842 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature