Functional comparison of RGS9 splice isoforms in a living cell

K.A. Martemyanov; C.M. Krispel; P.V. Lishko; M.E. Burns; V.Y. Arshavsky

doi:10.1073/pnas.0808941106

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Journal article

Functional comparison of RGS9 splice isoforms in a living cell

K.A. Martemyanov, C.M. Krispel, P.V. Lishko, M.E. Burns and V.Y. Arshavsky

Proceedings of the National Academy of Sciences of the United States of America, Vol.105(52), pp.20988-20993

2008

DOI: https://doi.org/10.1073/pnas.0808941106

PMID: 19098104

Abstract

G proteins

Phototransduction

RGS proteins

Alternative Splicing

Animals

Basal Ganglia

Behavior, Animal

Mice

Mice, Transgenic

Photoreceptor Cells, Vertebrate

Protein Isoforms

RGS Proteins

Transducin

Vision, Ocular

dopamine

guanine nucleotide binding protein

RGS protein

RGS9 protein

transducin

unclassified drug

animal cell

animal experiment

article

controlled study

female

mouse

nonhuman

photoactivation

priority journal

protein analysis

protein expression

protein function

protein protein interaction

quantitative analysis

retina rod

signal transduction

transgenic mouse

Two isoforms of the GTPase-activating protein, regulator of G protein signaling 9 (RGS9), control such fundamental functions as vision and behavior. RGS9-1 regulates phototransduction in rods and cones, and RGS9-2 regulates dopamine and opioid signaling in the basal ganglia. To determine their functional differences in the same intact cell, we replaced RGS9-1 with RGS9-2 in mouse rods. Surprisingly, RGS9-2 not only supported normal photoresponse recovery under moderate light conditions but also outperformed RGS9-1 in bright light. This versatility of RGS9-2 results from its ability to inactivate the G protein, transducin, regardless of its effector interactions, whereas RGS9-1 prefers the G protein-effector complex. Such versatility makes RGS9-2 an isoform advantageous for timely signal inactivation across a wide range of stimulus strengths and may explain its predominant representation throughout the nervous system. © 2008 by The National Academy of Sciences of the USA.

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Title: Functional comparison of RGS9 splice isoforms in a living cell
Creators: K.A. Martemyanov - University of Minnesota
C.M. Krispel - University of California, Davis
P.V. Lishko - Harvard University
M.E. Burns - University of California, Davis
V.Y. Arshavsky - Harvard University
Publication Details: Proceedings of the National Academy of Sciences of the United States of America, Vol.105(52), pp.20988-20993
Grant note: National Eye Institute: EY018139, EY14047, EY012859, EY012576, EY5722 Research to Prevent Blindness
We thank Edward N. Pugh for helpful comments on the manuscript, Norman A. Michaud for plastic sectioning, and Christopher Kessler and Peter Yoo for technical assistance. This work was supported by the National Eye Institute grants EY018139 (K. A. M.), EY14047 (M. E. B.), EY012859 (V. Y. A.), EY012576 (Core Grant for Vision Research to UC-Davis), and EY5722 (Core Grant for Vision Research to Duke University) and by Research to Prevent Blindness (M. E. B. and V. Y. A.).
Comment: Export Date: 24 October 2025; Cited By: 23; CODEN: PNASA
Academic Unit: Physiology and Biophysics Research; Miller School of Medicine
Resource Type: Journal article
PMID: 19098104
Record Identifier: 991032828879302976