A tale of two sites: How ubiquitination of a G protein-coupled receptor is coupled to its lysosomal trafficking from distinct receptor domains.

Journal Article (Journal Article)

The β(2)-adrenergic receptor (β(2)AR) is a prototypical G(s)-coupled receptor belonging to the superfamily of seven transmembrane spanning heptahelical receptors (7TMRs or G protein-coupled receptors [GPCRs])-therapeutically the most diverse and accessible class of cell surface receptors. The classic pathway of β(2)AR signaling (Fig. 1) is triggered by activation of the heterotrimeric G protein G(s) by agonists (catecholamines-noradrenaline and adrenaline). This in turn activates adenylyl cyclase leading to the generation of second messenger signaling molecules (cyclic adenosine monophosphates, cAMP) which subsequently activate protein kinase A (PKA) as well as some ion channels, such as the class C type of L-type calcium channels, Ca(v)1.2.31 Here in we review how trafficking and signaling of the β(2)AR is regulated by the post-translational modification, ubiquitination.1.

Full Text

Duke Authors

Cited Authors

  • Sarker, S; Xiao, K; Shenoy, SK

Published Date

  • September 2011

Published In

Volume / Issue

  • 4 / 5

Start / End Page

  • 528 - 531

PubMed ID

  • 22046454

Pubmed Central ID

  • PMC3204120

Electronic International Standard Serial Number (EISSN)

  • 1942-0889

Digital Object Identifier (DOI)

  • 10.4161/cib.4.5.16458


  • eng

Conference Location

  • United States