Β‐Arrestin‐1 directly interacts with Gαs and regulates its function. Issue 5 (23rd January 2013)

• Record Type: Journal Article
• Authors: Li, Bo; Wang, Congcong; Zhou, Zhaocai; Zhao, Jian; Pei, Gang
• Is Part Of: FEBS letters. Volume 587:Issue 5(2013)
• Page Start: 410
• Page End: 416
• Publication Date: 2013-01-23
• Subjects: βarr1 -- β-arrestin-1 -- DSP -- dithiobis[succinimidylpropionate] -- GDP -- guanosine 5′-diphosphate -- GPCR -- G protein-coupled receptor -- GTP -- guanosine 5′-triphosphate -- GTPγS -- gamma-thiol guanosine triphosphate -- β-Arrestin-1 -- G protein -- Interaction -- Biolayer interferometry analysis -- GTPγS binding and release; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.01.027
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Gαs physically interacts with Beta‐arrestin‐1 by cross‐linking study (View interaction). Abstract : ► We find β‐arrestin‐1 interacts with Gαs but not Gαi or Gαo . ► β‐Arrestin‐1 binds to Gαs in a rapid kinetic mode. ► β‐Arrestin‐1 promotes the binding and release of GTPγS from Gαs in vitro. ► The interaction deficient mutant β‐arrestin‐1 L33K has no detectable effects on the Gαs function.