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

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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.
Publisher
AMER CHEMICAL SOC
Issue Date
2002-03
Language
English
Article Type
Article
Keywords

BETA-ADRENERGIC-RECEPTOR; ROD OUTER SEGMENTS; BETA(2)-ADRENERGIC RECEPTOR; ARRESTIN/CLATHRIN INTERACTION; CLATHRIN ADAPTER; VISUAL ARRESTIN; 48-KDA PROTEIN; ENDOCYTOSIS; BINDING; ACTIVATION

Citation

BIOCHEMISTRY, v.41, no.10, pp.3321 - 3328

ISSN
0006-2960
DOI
10.1021/bi015905j
URI
http://hdl.handle.net/10203/240872
Appears in Collection
MSE-Journal Papers(저널논문)
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