Ser352 and Ser354 in the carboxyl terminus of the human P2Y(1) receptor are required for agonist-promoted phosphorylation and internalization in MDCK cells.

ABSTRACT:

Background and purpose

The P2Y(1) receptor promotes chloride secretion in epithelial cells, a process critical for regulation of extracellular ion and fluid levels. Here we have examined the role of phosphorylation in agonist-induced internalization of P2Y(1) receptors.

Experimental approach

A high-affinity radiolabelled antagonist, MRS2500, was used to quantify cell surface-binding sites of P2Y(1) receptors in Madin-Darby canine kidney (MDCK) epithelial cells, following exposure to agonists. The regions in the carboxyl terminus involved in both agonist-induced internalization of the receptor and its phosphorylation were identified by mutational analysis.

Key results

Endogenous and stably expressed recombinant P2Y(1) receptors rapidly internalized with similar time co

SUBMITTER: Qi AD 

PROVIDER: S-EPMC3058163 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature