Evidence map›Paper›PMID 28860193›Full record

ArticleThe Journal of biological chemistry2017

Structural and functional insights into the interaction between the Cas family scaffolding protein p130Cas and the focal adhesion-associated protein paxillin.

Chi Zhang, Darcie J Miller, Cristina D Guibao, Dominique M Donato, Steven K Hanks, Jie J Zheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. 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
1.1field-weighted citation impact, top 24% 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, 22 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. 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 3 institutions in 2 countries.

Chi ZhangFrom the Stein Eye Institute, Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, California 90095.
Darcie J MillerDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
Cristina D GuibaoDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
Dominique M DonatoDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, Tennessee 37232.
Steven K HanksDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, Tennessee 37232.ORCID 0000-0003-1414-5529
Jie J ZhengFrom the Stein Eye Institute, Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, California 90095, jzheng@jsei.ucla.edu.ORCID 0000-0001-6524-6800
St. Jude Children's Research Hospital · USLeiden University · NLVanderbilt University · US

Funding

Structural investigation of focal adhesion formation and disassemblyR01GM100909 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ZHENG, JIE J. · 2012 to 2015
$1.5M
NIGMS NIH HHS R01 GM100909
6 · The paper itself

Abstract

The Cas family scaffolding protein p130Cas is a Src substrate localized in focal adhesions (FAs) and functions in integrin signaling to promote cell motility, invasion, proliferation, and survival. p130Cas targeting to FAs is essential for its tyrosine phosphorylation and downstream signaling. Although the N-terminal SH3 domain is important for p130Cas localization, it has also been reported that the C-terminal region is involved in p130Cas FA targeting. The C-terminal region of p130Cas or Cas family homology domain (CCHD) has been reported to adopt a structure similar to that of the focal adhesion kinase C-terminal focal adhesion-targeting domain. The mechanism by which the CCHD promotes FA targeting of p130Cas, however, remains unclear. In this study, using a calorimetry approach, we identified the first LD motif (LD1) of the FA-associated protein paxillin as the binding partner of the p130Cas CCHD (in a 1:1 stoichiometry with a

Indexed as

Models, MolecularAmino Acid MotifsAmino Acid SubstitutionAnimalsAvian ProteinsBinding SitesChickensCrk-Associated Substrate ProteinCrystallography, X-RayHydrophobic and Hydrophilic InteractionsKineticsLeucineMiceMutationPaxillinPeptide FragmentsAvian ProteinsBcar1 protein, mouseCrk-Associated Substrate ProteinLeucinePaxillinPeptide FragmentsRecombinant Proteinsfocal adhesionnuclear magnetic resonance (NMR)p130Cas/BCAR1paxillinPTK2 protein tyrosine kinase 2 (PTK2) (focal adhesion kinase) (FAK)scaffold proteinX-ray crystallography

Identifiers

PMID28860193
PMCPMC5672050
OpenAlexW2753484764

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.