Identification and characterization of distinct C-terminal domains of the human hydroxycarboxylic acid receptor-2 that are essential for receptor export, constitutive activity, desensitization, and internalization.

ABSTRACT: The human hydroxycarboxylic acid receptor 2 (HCA₂), also known as GPR109A and HM74a, was first identified as a niacin receptor and has recently received significant attention because of its potential to clinically modify plasma lipids in a favorable manner. Our recent studies have demonstrated that the niacin-induced internalization of HCA₂ receptors is regulated by G protein-coupled receptor kinase (GRK) 2 and arrestin3 and that internalized receptors rapidly recycle back to the cell surface. The investigation presented here used a combination of amino acid deletion and site-directed mutagenesis to identify structural and functional domains within the HCA₂ C terminus and explore their potential roles in receptor phosphorylation, desensitization, and internalization. We first constructed f

SUBMITTER: Li G 

PROVIDER: S-EPMC3502627 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature