Evidence map›Paper›PMID 20430886›Full record

ArticleThe Journal of biological chemistry2010

Activated RhoA binds to the pleckstrin homology (PH) domain of PDZ-RhoGEF, a potential site for autoregulation.

Zhe Chen, Frank Medina, Mu-ya Liu, Celestine Thomas, Stephen R Sprang, Paul C Sternweis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

47 citing papers in PubMed, 78 citations in OpenAlex.

  1. Structural basis for membrane-dependent positive feedback regulation of DOCK11 by activated Cdc42.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Identification ofProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024
    Review
  11. Genotype-phenotype correlations in RHOBTB2-associated neurodevelopmental disorders.Genetics in medicine : official journal of the American College of Medical Genetics · 2023
    Article
  12. Article
  13. Article
  14. GαThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Zhe ChenDepartment of Pharmacology, The University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Zhe.Chen@utsouthwestern.edu
Frank Medina
Mu-ya Liu
Celestine Thomas
Stephen R Sprang
Paul C Sternweis
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

Guanine nucleotide exchange factors (GEFs) catalyze exchange of GDP for GTP by stabilizing the nucleotide-free state of the small GTPases through their Dbl homology/pleckstrin homology (DH.PH) domains. Unconventionally, PDZ-RhoGEF (PRG), a member of the RGS-RhoGEFs, binds tightly to both nucleotide-free and activated RhoA (RhoA.GTP). We have characterized the interaction between PRG and activated RhoA and determined the structure of the PRG-DH.PH-RhoA.GTPgammaS (guanosine 5'-O-[gamma-thio]triphosphate) complex. The interface bears striking similarity to a GTPase-effector interface and involves the switch regions in RhoA and a hydrophobic patch in PRG-PH that is conserved among all Lbc RhoGEFs. The two surfaces that bind activated and nucleotide-free RhoA on PRG-DH.PH do not overlap, and a ternary complex of PRG-DH.PH bound to both forms of RhoA can be isolated by size-exclusion chromatography. This novel interaction between activated RhoA and PH could play a key role in regulation of RhoGEF activity in vivo.

Indexed as

Binding SitesChromatography, GelCloning, MolecularCrystallography, X-RayEnzyme ActivationEscherichia coliGenetic VectorsGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateHomeostasisHumansKineticsPeptide FragmentsrhoA GTP-Binding ProteinARHGEF11 protein, humanGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphatePeptide FragmentsrhoA GTP-Binding ProteinRho Guanine Nucleotide Exchange Factors

Identifiers

PMID20430886
PMCPMC2898337
OpenAlexW2046697062

What OpenQuestion holds

Textmetadata
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.