Adaptor protein-2 interaction with arrestin regulates GPCR recycling and apoptosis.

ABSTRACT: G protein-coupled receptors (GPCRs) are integral to cellular function in nearly all physiologic and many pathologic processes. GPCR signaling represents an intricate balance between receptor activation, inactivation (desensitization, internalization and degradation) and resensitization (recycling and de novo synthesis). Complex formation between phosphorylated GPCRs, arrestins and an ever-increasing number of effector molecules is known to regulate cellular function. Previous studies have demonstrated that, although N-formyl peptide receptor (FPR) internalization occurs in the absence of arrestins, FPR recycling is arrestin-dependent. Furthermore, FPR stimulation in the absence of arrestins leads to receptor accumulation in perinuclear endosomes and apoptosis. In this study, we show that t

SUBMITTER: Wagener BM 

PROVIDER: S-EPMC2923382 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature