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

Cited 148 time in webofscience Cited 0 time in scopus
  • Hit : 189
  • Download : 0
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)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 148 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0