Journal
BIOCHEMISTRY
Volume 41, Issue 10, Pages 3321-3328Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi015905j
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Funding
- NCI NIH HHS [T32 CA 07403] Funding Source: Medline
- NIGMS NIH HHS [GM 47417] Funding Source: Medline
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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.
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