Publication Abstract from PubMed
Arrestin binding to activated, phosphorylated G protein-coupled receptors (GPCRs) represents a critical step in regulation of light- and hormone-dependent signaling. Nonvisual arrestins, such as arrestin-2, interact with multiple proteins for the purpose of propagating and terminating signaling events. Using a combination of X-ray crystallography, molecular modeling, mutagenesis, and binding analysis, we reveal structural features of arrestin-2 that may enable simultaneous binding to phosphorylated receptor, SH3 domains, phosphoinositides, and beta-adaptin. The structure of full-length arrestin-2 thus provides a uniquely oriented scaffold for assembly of multiple, diverse molecules involved in GPCR signal transduction.
Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis.,Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL Biochemistry. 2002 Mar 12;41(10):3321-8. PMID:11876640[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
