Evidence map›Paper›PMID 18940608›Full record

ArticleStructure (London, England : 1993)2008

Recognition of the activated states of Galpha13 by the rgRGS domain of PDZRhoGEF.

Zhe Chen, William D Singer, Shahab M Danesh, Paul C Sternweis, Stephen R Sprang

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Stabilization of interdomain closure by a G protein inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Article
  5. A network of GαScience signaling · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Tyrosine phosphorylation switching of a G protein.The Journal of biological chemistry · 2018
    Article
  10. Mechanism of the intrinsic arginine finger in heterotrimeric G proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Review
  13. Probing Gαi1 protein activation at single-amino acid resolution.Nature structural & molecular biology · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Zhe ChenDepartment of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
William D Singer
Shahab M Danesh
Paul C Sternweis
Stephen R Sprang
The University of Texas Southwestern Medical Center · USUniversity of Montana · US

Funding

TRANSMEMEBRANE SIGNALING VIA RECEPTORS AND G PROTEINSR01GM031954 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI STERNWEIS, PAUL C · 1985 to 2017
$7.1M
X RAY STRUCTURE DETERMINATION OF G PROTEIN A SUBUNITSR01DK046371 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI SPRANG, STEPHEN R. · 1994 to 2007
$2.1M
Structural Analysis of G Protein Regulatory MechanismsR56DK046371 · NIDDK · UNIVERSITY OF MONTANA · PI SPRANG, STEPHEN R · 2009 to 2009
$133k
NIDDK NIH HHS DK46371NIDDK NIH HHS R01 DK046371NIDDK NIH HHS R56 DK046371NIGMS NIH HHS GM31954NIGMS NIH HHS R01 GM031954
6 · The paper itself

Abstract

G12 class heterotrimeric G proteins stimulate RhoA activation by RGS-RhoGEFs. However, p115RhoGEF is a GTPase Activating Protein (GAP) toward Galpha13, whereas PDZRhoGEF is not. We have characterized the interaction between the PDZRhoGEF rgRGS domain (PRG-rgRGS) and the alpha subunit of G13 and have determined crystal structures of their complexes in both the inactive state bound to GDP and the active states bound to GDP*AlF (transition state) and GTPgammaS (Michaelis complex). PRG-rgRGS interacts extensively with the helical domain and the effector-binding sites on Galpha13 through contacts that are largely conserved in all three nucleotide-bound states, although PRG-rgRGS has highest affinity to the Michaelis complex. An acidic motif in the N terminus of PRG-rgRGS occupies the GAP binding site of Galpha13 and is flexible in the GDP*AlF complex but well ordered in the GTPgammaS complex. Replacement of key residues in this motif with their counterparts in p115RhoGEF confers GAP activity.

Indexed as

Amino Acid SequenceAnimalsGTPase-Activating ProteinsGTP-Binding Protein alpha Subunits, G12-G13Guanine Nucleotide Exchange FactorsGuanosine 5'-O-(3-Thiotriphosphate)MiceModels, MolecularMolecular Sequence DataProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein Structure, TertiaryRatsRGS ProteinsSequence Homology, Amino AcidGTPase-Activating ProteinsGTP-Binding Protein alpha Subunits, G12-G13Guanine Nucleotide Exchange FactorsGuanosine 5'-O-(3-Thiotriphosphate)PDZ-RhoGEF, ratRGS Proteins

Identifiers

PMID18940608
PMCPMC2586972
OpenAlexW2019491840

What OpenQuestion holds

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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.