Evidence map›Paper›PMID 35970859›Full record

ArticleNature communications2022

SH3 domain regulation of RhoGAP activity: Crosstalk between p120RasGAP and DLC1 RhoGAP.

Jocelyn E Chau, Kimberly J Vish, Titus J Boggon, Amy L Stiegler

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Clinically observedbioRxiv : the preprint server for biology · 2025
    Article
  6. Nickel binding to c-Src SH3 domain facilitates crystallization.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Dynamic regulation of RAS and RAS signaling.The Biochemical journal · 2023
    Article
  14. 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

4 authors at 1 institution in 1 country.

Jocelyn E ChauDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.
Kimberly J VishDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0002-9394-1218
Titus J BoggonDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA.ORCID 0000-0003-2862-1637
Amy L StieglerDepartment of Pharmacology, Yale University, New Haven, CT, USA. amy.stiegler@yale.edu.ORCID 0000-0003-0453-6104
Yale University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI STEVEN E EALICK · 2018 to 2026
$34.2M
PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
Human Genetics and Molecular Mechanisms of Vein of Galen Aneurysmal MalformationR01NS117609 · NINDS · YALE UNIVERSITY · PI Titus Jonathon Boggon, Kristopher T. Kahle · 2020 to 2026
$3.3M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
P21-activated kinases in cell-cell and cell-matrix adhesion signalingR01GM138411 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, CALDERWOOD, DAVID A · 2020 to 2023
$1.7M
NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM138411NIGMS NIH HHS T32 GM008283NIH HHS S10 OD021527NINDS NIH HHS R01 NS117609
6 · The paper itself

Abstract

RhoGAP proteins are key regulators of Rho family GTPases and influence a variety of cellular processes, including cell migration, adhesion, and cytokinesis. These GTPase activating proteins (GAPs) downregulate Rho signaling by binding and enhancing the intrinsic GTPase activity of Rho proteins. Deleted in liver cancer 1 (DLC1) is a tumor suppressor and ubiquitously expressed RhoGAP protein; its activity is regulated in part by binding p120RasGAP, a GAP protein for the Ras GTPases. In this study, we report the co-crystal structure of the p120RasGAP SH3 domain bound directly to DLC1 RhoGAP, at a site partially overlapping the RhoA binding site and impinging on the catalytic arginine finger. We demonstrate biochemically that mutation of this interface relieves inhibition of RhoGAP activity by the SH3 domain. These results reveal the mechanism for inhibition of DLC1 RhoGAP activity by p120RasGAP and demonstrate the molecular basis for direct SH3 domain modulation of GAP activity.

Indexed as

p120 GTPase Activating Proteinsrc Homology DomainsGTPase-Activating Proteinsrho GTP-Binding ProteinsTumor Suppressor ProteinsGTPase-Activating Proteinsp120 GTPase Activating Proteinrho GTPase-activating proteinrho GTP-Binding ProteinsTumor Suppressor Proteins

Identifiers

PMID35970859
PMCPMC9378701
OpenAlexW4291782152

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.