Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Filters applied. Clear all
, 41 (10), 3321-8

Scaffolding Functions of arrestin-2 Revealed by Crystal Structure and Mutagenesis

Affiliations

Scaffolding Functions of arrestin-2 Revealed by Crystal Structure and Mutagenesis

Shawn K Milano et al. Biochemistry.

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.

Similar articles

See all similar articles

Cited by 70 articles

See all "Cited by" articles

Publication types

Associated data

LinkOut - more resources

Feedback