Evidence map›Paper›PMID 23434405›Full record

ArticleStructure (London, England : 1993)2013

Structural and functional analysis of the regulator of G protein signaling 2-gαq complex.

Mark R Nance, Barry Kreutz, Valerie M Tesmer, Rachel Sterne-Marr, Tohru Kozasa, John J G Tesmer

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 65 citations in OpenAlex.

  1. GαThe FEBS journal · 2025
    Article
  2. Selective optogenetic inhibition of GαProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. RGS2 and female common diseases: a guard of women's health.Journal of translational medicine · 2023
    Review
  5. Article
  6. Regulator of G protein signaling 2 inhibits GαThe Journal of biological chemistry · 2022
    Article
  7. Novel Molecular Targets of Antidepressants.Molecules (Basel, Switzerland) · 2022
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. High-resolution structure of RGS17 suggests a role for CaThe Journal of biological chemistry · 2019
    Article
  17. Article
  18. Article
  19. Atypical activation of the G protein GαThe Journal of biological chemistry · 2018
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Mark R NanceLife Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216, USA.
Barry Kreutz
Valerie M Tesmer
Rachel Sterne-Marr
Tohru Kozasa
John J G Tesmer
University of Michigan · USUniversity of Illinois Urbana-Champaign · USSiena College · US

Funding

PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
Structure, function, and inhibition of G protein-coupled receptor kinasesR01HL071818 · NHLBI · UNIVERSITY OF TEXAS AUSTIN · PI TESMER, JOHN · 2004 to 2023
$7.1M
Regulation of Rho family GTPases by heterotrimeric G proteinsR01GM061454 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI KOZASA, TOHRU, KREUTZ, BARRY S. · 1999 to 2014
$3.3M
Structural Studies of Galphaq and Its Complexes at the Cell MembraneR01HL086865 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESMER, JOHN · 2007 to 2015
$3.0M
Regulation of G Protein Signaling by RGS ProteinsR01GM074001 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI KOZASA, TOHRU · 2008 to 2011
$1.2M
NHLBI NIH HHS HL071818NHLBI NIH HHS HL086865NHLBI NIH HHS R01 HL071818NHLBI NIH HHS R01 HL086865NIDDK NIH HHS DK20572NIDDK NIH HHS P30 DK020572NIDDK NIH HHS P60 DK020572NIGMS NIH HHS GM061454NIGMS NIH HHS GM074001NIGMS NIH HHS R01 GM061454NIGMS NIH HHS R01 GM074001
6 · The paper itself

Abstract

The heterotrimeric G protein Gαq is a key regulator of blood pressure, and excess Gαq signaling leads to hypertension. A specific inhibitor of Gαq is the GTPase activating protein (GAP) known as regulator of G protein signaling 2 (RGS2). The molecular basis for how Gαq/11 subunits serve as substrates for RGS proteins and how RGS2 mandates its selectivity for Gαq is poorly understood. In crystal structures of the RGS2-Gαq complex, RGS2 docks to Gαq in a different orientation from that observed in RGS-Gαi/o complexes. Despite its unique pose, RGS2 maintains canonical interactions with the switch regions of Gαq in part because its α6 helix adopts a distinct conformation. We show that RGS2 forms extensive interactions with the α-helical domain of Gαq that contribute to binding affinity and GAP potency. RGS subfamilies that do not serve as GAPs for Gαq are unlikely to form analogous stabilizing interactions.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceAnimalsBinding SitesCattleCrystallography, X-RayEscherichia coliGTP-Binding Protein alpha Subunits, Gq-G11HumansMiceMolecular Docking SimulationMolecular Sequence DataMutationProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryGTP-Binding Protein alpha Subunits, Gq-G11Protein SubunitsRecombinant ProteinsRGS2 protein, humanRGS Proteins

Identifiers

PMID23434405
PMCPMC3638996
OpenAlexW2063308273

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.