Interaction of human retinal RGS with G‐protein α‐subunits

FEBS Letters

Lipkin, Valery M²  Natochin, Michael¹  Artemyev, Nikolai O¹ 

[1] Department of Physiology and Biophysics, University of Iowa College of Medicine, 5-660 BSB, Iowa City, IA 52242, USA;Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117871, Russia

关键词: G-protein;    Transducin;    Regulator of G-protein signaling;    Retina;    G α;    heterotrimeric GTP-binding protein α-subunit;    PDE;    photoreceptor cGMP phosphodiesterase;    Gtα β γ;    rod G-protein;    transducin;    RGS proteins;    regulators of G-protein signaling;    hRGSr;    human retinal RGS protein;   

DOI  :  10.1016/S0014-5793(97)00687-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel family of RGS proteins negatively regulates signaling via heterotrimeric G-proteins by accelerating the GTPase activity of G-protein α subunits. We have investigated interaction of human retinal RGS protein (hRGSr) with in vitro translated G _α subunits: G_tα , G_iα1, G_oα and G_sα . hRGSr binds well to G_tα , G_iα1 and G_oα in the presence of AlF₄ ⁻, but does not interact with G_sα . The N- and C-terminally truncated G _α subunits interact with hRGSr similarly to the intact G _α polypeptides. Analysis of interaction between hRGSr and G_oα /G_sα chimeras suggests that a region of G_oα , G_oα 22–212, contains major structural determinants for binding to RGS proteins.

【 授权许可】

Unknown