Evidence map›Paper›PMID 11238453›Full record

ArticleThe Journal of cell biology2001

Regulation of CDC42 GTPase by proline-rich tyrosine kinase 2 interacting with PSGAP, a novel pleckstrin homology and Src homology 3 domain containing rhoGAP protein.

X R Ren, Q S Du, Y Z Huang, S Z Ao, L Mei, W C Xiong

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 123 citations in OpenAlex.

  1. Trial
  2. Functional genomics iniScience · 2026
    Article
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  4. Article
  5. Platelet spreading and clot retraction are regulated by 2 distinct αThe Journal of pharmacology and experimental therapeutics · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022
    Review
  10. Article
  11. Article
  12. Myosin X Interaction with KIF13B, a Crucial Pathway for Netrin-1-Induced Axonal Development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Role of Pyk2 in Human Cancers.Medical science monitor : international medical journal of experimental and clinical research · 2018
    Review
  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 2 countries.

X R RenDepartment of Pathology and Cell Adhesion and Matrix Center, Pathology, and Physical Medicine and Rehabilitation, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
Q S Du
Y Z Huang
S Z Ao
L Mei
W C Xiong
University of Alabama at Birmingham · USCenter for Excellence in Molecular Cell Science · CN

Funding

SIGNALING MECHANISMS REGULATING ACHR SYNTHESIS AT NMJR01NS040480 · NINDS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MEI, LIN · 2000 to 2013
$3.6M
PROTEIN TYROSINE PHOSPHATASES AT NEUROMUSCULAR JUNCTIONR29NS034062 · NINDS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI MEI, LIN · 1995 to 1999
–
NINDS NIH HHS NS34062NINDS NIH HHS NS40480NINDS NIH HHS R01 NS040480
6 · The paper itself

Abstract

Proline-rich tyrosine kinase 2 (PYK2), a tyrosine kinase structurally related to focal adhesion kinase (FAK), is implicated in regulating cytoskeletal organization. However, mechanisms by which PYK2 participates in and regulates cytoskeletal organization remain largely unknown. Here we report identification of PSGAP, a novel protein that interacts with PYK2 and FAK and contains multiple domains including a pleckstrin homology domain, a rhoGTPase-activating protein domain, and a Src homology 3 domain. PYK2 interacts with PSGAP Src homology 3 domain via the carboxyl-terminal proline-rich sequence. PSGAP is able to increase GTPase activity of CDC42 and RhoA in vitro and in vivo. Remarkably, PYK2, but not FAK, can activate CDC42 via inhibition of PSGAP-mediated GTP hydrolysis of CDC42. Moreover, PSGAP is localized at cell periphery in fibroblasts in a pleckstrin homology domain-dependent manner. Over expression of PSGAP in fibroblasts results in reorganization of cytoskeletal structures and changes of cellular morphology, which requires rhoGTPase-activating activity. Taken together, our results suggest that PSGAP is a signaling protein essential for PYK2 regulation of cytoskeletal organization via Rho family GTPases.

Indexed as

src Homology DomainsAmino Acid SequenceBlood Proteinscdc42 GTP-Binding ProteinCell LineCloning, MolecularCytoskeletonEnzyme ActivationFibroblastsFocal Adhesion Kinase 1Focal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesGTPase-Activating ProteinsHumansMolecular Sequence DataPhosphoproteinsARHGAP10 protein, humanArhgap10 protein, mouseARHGAP26 protein, humanBlood Proteinscdc42 GTP-Binding ProteinFocal Adhesion Kinase 1Focal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesGTPase-Activating ProteinsPhosphoproteinsplatelet protein P47ProlineProtein-Tyrosine KinasesPTK2 protein, humanran GTP-Binding ProteinrhoA GTP-Binding Proteinrho GTPase-activating protein

Identifiers

PMID11238453
PMCPMC2198805
OpenAlexW2030192350

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.