Evidence map›Paper›PMID 34006635›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Structural basis for p50RhoGAP BCH domain-mediated regulation of Rho inactivation.

Vishnu Priyanka Reddy Chichili, Ti Weng Chew, Srihari Shankar, Shi Yin Er, Cheen Fei Chin, Chacko Jobichen, Catherine Qiurong Pan, Yiting Zhou, Foong May Yeong, Boon Chuan Low and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
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  4. How Functional Variants Reconfigure the Rac2 Conformational Landscape.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Review
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  9. Article
  10. Article
  11. Article
  12. Article
  13. Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022
    Review
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

11 authors at 1 institution in 1 country.

Vishnu Priyanka Reddy ChichiliDepartment of Biological Sciences, National University of Singapore, Singapore 117543.
Ti Weng ChewMechanobiology Institute, National University of Singapore, Singapore 117411.ORCID 0000-0002-5898-4722
Srihari ShankarDepartment of Biological Sciences, National University of Singapore, Singapore 117543.ORCID 0000-0003-2540-969X
Shi Yin ErDepartment of Biological Sciences, National University of Singapore, Singapore 117543.ORCID 0000-0003-2871-6388
Cheen Fei ChinDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117596.
Chacko JobichenDepartment of Biological Sciences, National University of Singapore, Singapore 117543.ORCID 0000-0001-5927-1815
Catherine Qiurong PanMechanobiology Institute, National University of Singapore, Singapore 117411.
Yiting ZhouMechanobiology Institute, National University of Singapore, Singapore 117411.
Foong May YeongDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117596.
Boon Chuan LowDepartment of Biological Sciences, National University of Singapore, Singapore 117543; dbslowbc@nus.edu.sg dbsjayar@nus.edu.sg.
J SivaramanDepartment of Biological Sciences, National University of Singapore, Singapore 117543; dbslowbc@nus.edu.sg dbsjayar@nus.edu.sg.
National University of Singapore · SG

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
NIGMS NIH HHS P30 GM124165
6 · The paper itself

Abstract

Spatiotemporal regulation of signaling cascades is crucial for various biological pathways, under the control of a range of scaffolding proteins. The BNIP-2 and Cdc42GAP Homology (BCH) domain is a highly conserved module that targets small GTPases and their regulators. Proteins bearing BCH domains are key for driving cell elongation, retraction, membrane protrusion, and other aspects of active morphogenesis during cell migration, myoblast differentiation, and neuritogenesis. We previously showed that the BCH domain of p50RhoGAP (ARHGAP1) sequesters RhoA from inactivation by its adjacent GAP domain; however, the underlying molecular mechanism for RhoA inactivation by p50RhoGAP remains unknown. Here, we report the crystal structure of the BCH domain of p50RhoGAP

Indexed as

Amino Acid SequenceCarrier Proteinscdc42 GTP-Binding ProteinCell DifferentiationCell LineCell MovementEndocytosisGTPase-Activating ProteinsHumansMorphogenesisProtein BindingProtein Structure, TertiaryrhoA GTP-Binding ProteinSchizosaccharomycesSequence Homology, Amino AcidSignal TransductionArhgap1 protein, mouseBNIP2 protein, humanCarrier Proteinscdc42 GTP-Binding ProteinGTPase-Activating ProteinsrhoA GTP-Binding ProteinRHOA protein, humanBCH domainGTPase-activating proteinRhoSec14signaling

Identifiers

PMID34006635
PMCPMC8166187
OpenAlexW3160525161

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.