Affordable Access

Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis.

Authors
Type
Published Article
Journal
Biochemistry
Publication Date
Volume
41
Issue
10
Pages
3321–3328
Identifiers
PMID: 11876640
Source
Medline
License
Unknown

Abstract

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.

Statistics

Seen <100 times