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 journalArticle

142 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)7216-7220
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number14
DOIs
StatePublished - Jul 8 1997

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GTPase-Activating Proteins
GTP-Binding Proteins
RGS Proteins
Surface Plasmon Resonance
GTP Phosphohydrolases
Guanosine Triphosphate
Amino Acid Sequence
Proteins
Hydrolysis
In Vitro Techniques
Protein Domains

Keywords

  • Densitization
  • GTP hydrolysis

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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T1 - The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro

AU - Popov, Serguei

AU - Yu, Kan

AU - Kozasa, Tohru

AU - Wilkie, Thomas M.

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N2 - 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.

AB - 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.

KW - Densitization

KW - GTP hydrolysis

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