The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro

Serguei Popov; Kan Yu; Tohru Kozasa; Thomas M. Wilkie

doi:10.1073/pnas.94.14.7216

The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro

Serguei Popov, Kan Yu, Tohru Kozasa, Thomas M. Wilkie

Research output: Contribution to journal › Article › peer-review

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Abstract

Regulators of G protein signaling (RGS) proteins accelerate GTP hydrolysis by G(i) but not by G(s) class α-subunits. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. We have demonstrated thai the RGS domains of RGS4, RGS10, and GAIP retain GTPase accelerating activity with the G(i) class substrates G(iα1) G(oα), and G(zα) in vitro. No regulatory activity of the RGS domains was detected for G(sα). Short deletions within the RGS domain of RGS4 destroyed GTPase activating protein activity and G(iα1) substrate binding. Comparable protein-protein interactions between G(iα1)-GDP-AlF₄/^- and the RGS domain or full-length RGS4 were detected using surface plasmon resonance.

Original language	English (US)
Pages (from-to)	7216-7220
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	94
Issue number	14
DOIs	https://doi.org/10.1073/pnas.94.14.7216
State	Published - Jul 8 1997

Keywords

Densitization
GTP hydrolysis

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The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro. / Popov, Serguei; Yu, Kan; Kozasa, Tohru et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, No. 14, 08.07.1997, p. 7216-7220.

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The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro

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Keywords

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