Heterologous regulation of agonist-independent μ-opioid receptor phosphorylation by protein kinase C.

ABSTRACT:

Background and purpose

Homologous agonist-induced phosphorylation of the μ-opioid receptor (MOR) is initiated at the carboxyl-terminal S375, followed by phosphorylation of T370, T376 and T379. In HEK293 cells, this sequential and hierarchical multi-site phosphorylation is specifically mediated by G-protein coupled receptor kinases 2 and 3. In the present study, we provide evidence for a selective and dose-dependent phosphorylation of T370 after activation of PKC by phorbol esters.

Experimental approach

We used a combination of phospho site-specific antibodies, kinase inhibitors and siRNA knockdown screening to identify kinases that mediate agonist-independent phosphorylation of the MOR in HEK293 cells. In addition, we show with phospho site-specific antibodies were also used

SUBMITTER: Illing S 

PROVIDER: S-EPMC3952808 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature