Agonist-selective patterns of µ-opioid receptor phosphorylation revealed by phosphosite-specific antibodies.

ABSTRACT:

Background and purpose

Morphine activates the µ-opioid receptor without causing its rapid endocytosis. In contrast, full agonists such as [d-Ala(2) -MePhe(4) -Gly-ol]enkephalin (DAMGO) or etonitazene stimulate a rapid and profound internalization. However, the detailed molecular events underlying the differential regulation of receptor trafficking by distinct opioid agonists remain incompletely understood.

Experimental approach

Here, we have generated phosphosite-specific antibodies for the carboxyl-terminal residues serine 363 (Ser363), threonine 370 (Thr370) and serine 375 (Ser375), which enabled us to selectively detect either the Ser363-, Thr370- or Ser375-phosphorylated form of the receptor.

Key results

We showed that agonist-induced phosphorylation occurs at Thr

SUBMITTER: Doll C 

PROVIDER: S-EPMC3174411 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature