Journal article
Interaction of human retinal RGS with G-protein α-subunits
FEBS letters, Vol.411(2), pp.179-182
1997
DOI: 10.1016/S0014-5793(97)00687-X
PMID: 9271201
Abstract
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
t
α
, G
i
α1
, G
o
α
and G
s
α
. hRGSr binds well to G
t
α
, G
i
α1
and G
o
α
in the presence of AlF
4
−, but does not interact with G
s
α
. 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
o
α
/G
s
α
chimeras suggests that a region of G
o
α
, G
o
α
22–212, contains major structural determinants for binding to RGS proteins.
Details
- Title: Subtitle
- Interaction of human retinal RGS with G-protein α-subunits
- Creators
- Michael Natochin - Department of Physiology and Biophysics, University of Iowa College of Medicine, 5-660 BSB, Iowa City, IA 52242, USAValery M Lipkin - Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117871, RussiaNikolai O Artemyev - Department of Physiology and Biophysics, University of Iowa College of Medicine, 5-660 BSB, Iowa City, IA 52242, USA
- Resource Type
- Journal article
- Publication Details
- FEBS letters, Vol.411(2), pp.179-182
- Publisher
- Elsevier B.V
- DOI
- 10.1016/S0014-5793(97)00687-X
- PMID
- 9271201
- ISSN
- 0014-5793
- eISSN
- 1873-3468
- Language
- English
- Date published
- 1997
- Academic Unit
- Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Ophthalmology and Visual Sciences
- Record Identifier
- 9984025354202771
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