Interaction of human retinal RGS with G-protein alpha-subunits.
A novel family of RGS proteins negatively regulates signaling via heterotrimeric G-proteins by accelerating the GTPase activity of G-protein alpha subunits. We have investigated interaction of human retinal RGS protein (hRGSr) with in vitro translated G(alpha) subunits: G(t alpha), G(i alpha1), G(o alpha) and G(s alpha). hRGSr binds well to G(t alpha), G(i alpha1) and G(o alpha) in the presence of AIF4-, but does not interact with G(s alpha). The N- and C-terminally truncated G(alpha) subunits interact with hRGSr similarly to the intact G(alpha) polypeptides. Analysis of interaction between hRGSr and G(o alpha)/G(s alpha) chimeras suggests that a region of G(o alpha), G(o alpha)22-212, contains major structural determinants for binding to RGS proteins.
Natochin
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Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City 52242, USA.
Lipkin
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VM
Artemyev
N O
NO
D017607:Aluminum Compounds / Q000378:metabolism; D000818:Animals; D002417:Cattle; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D005136:Eye Proteins / Q000235:genetics / Q000378:metabolism*; D005459:Fluorides / Q000378:metabolism; D020558:GTP Phosphohydrolases / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D020710:RGS Proteins; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012374:Rod Cell Outer Segment / Q000737:chemistry; D015293:Transducin / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D017607:Aluminum Compounds; D005136:Eye Proteins; D020710:RGS Proteins; C107413:RGS16 protein; D011993:Recombinant Fusion Proteins; C050992:tetrafluoroaluminate; D006160:Guanosine Triphosphate; D014357:Trypsin; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins; D015293:Transducin; D005459:Fluorides