Publication
Title
-arrestin-dependent formation of adrenergic receptor Src protein kinase complexes
Author
Abstract
The Pas-dependent activation of mitogen-activated protein (MAP) kinase pathways by many receptors coupled to heterotrimeric guanine nucleotide binding proteins (G proteins) requires the activation of Src family tyrosine kinases. Stimulation of beta(2) adrenergic receptors resulted in the assembly of a protein complex containing activated c-Src and the receptor. Src recruitment was mediated by beta-arrestin, which functions as an adapter protein, binding both c-Src and the agonist-occupied receptor. beta-Arrestin 1 mutants, impaired either in c-Src binding or in the ability to target receptors to clathrin-coated pits, acted as dominant negative inhibitors of beta(2) adrenergic receptor-mediated activation of the MAP kinases Erk1 and Erk2. These data suggest that beta-arrestin binding, which terminates receptor-C protein;coupling, also initiates a second wave of signal transduction in which the "desensitized" receptor functions as a critical structural component of a mitogenic signaling complex.
Language
English
Source (journal)
Science / American Association for the Advancement of Science [Washington, D.C.] - Washington, D.C.
Publication
Washington, D.C. : 1999
ISSN
0036-8075
1095-9203
Volume/pages
283:5402(1999), p. 655-661
ISI
000078324400032
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Faculty/Department
Project info
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 06.01.2015
Last edited 30.11.2017