Modulation of Cl^- signaling and ion transport by recruitment of kinases and phosphatases mediated by the regulatory protein IRBIT.

ABSTRACT: IRBIT is a multifunctional protein that controls the activity of various epithelial ion transporters including NBCe1-B. Interaction with IRBIT increases NBCe1-B activity and exposes two cryptic Cl^--sensing GXXXP sites that enable regulation of NBCe1-B by intracellular Cl^- (Cl^- _in). Here, phosphoproteomic analysis revealed that IRBIT controlled five phosphorylation sites in NBCe1-B that determined both the active conformation of the transporter and its regulation by Cl^- _in Mutational analysis suggested that the phosphorylation status of Ser²³², Ser²³³, and Ser²³⁵ was regulated by IRBIT and determined whether NBCe1 transporters are in active or inactive conformations. The absence of phosphoryla

SUBMITTER: Vachel L 

PROVIDER: S-EPMC8325875 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature