Evidence map›Paper›PMID 27150043›Full record

ArticleStructure (London, England : 1993)2016

Structural and Functional Analysis of a Talin Triple-Domain Module Suggests an Alternative Talin Autoinhibitory Configuration.

Hao Zhang, Yu-Chung Chang, Qingqiu Huang, Mark L Brennan, Jinhua Wu

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. 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
1.9field-weighted citation impact, top 16% 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, 20 citations in OpenAlex.

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  7. Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

5 authors at 2 institutions in 1 country.

Hao ZhangMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.
Yu-Chung ChangMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.
Qingqiu HuangMacCHESS, Cornell University, Ithaca, NY 14853, USA.
Mark L BrennanMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.
Jinhua WuMolecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111, USA. Electronic address: jinhua.wu@fccc.edu.
Fox Chase Cancer Center · USCornell University · US

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Dietmar J Kappes · 1985 to 2026
$138.8M
Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
NCI NIH HHS P30 CA006927NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

Talin plays an important role in regulating integrin-mediated signaling. Talin function is autoinhibited by intramolecular interactions between the integrin-binding F3 domain and the autoinhibitory domain (R9). We determined the crystal structure of a triple-domain fragment, R7R8R9, which contains R9 and the RIAM (Rap1-interacting adaptor molecule) binding domain (R8). The structure reveals a crystallographic contact between R9 and a symmetrically related R8 domain, representing a homodimeric interaction in talin. Strikingly, we demonstrated that the α5 helix of R9 also interacts with the F3 domain, despite no interdomain contact involving the α5 helix in the crystal structure of an F2F3:R9 autoinhibitory complex reported previously. Mutations on the α5 helix significantly diminish the F3:R9 association and lead to elevated talin activity. Our results offer biochemical and functional evidence of the existence of a new talin autoinhibitory configuration, thus providing a more comprehensive understanding of talin autoinhibition, regulation, and quaternary structure assembly.

Indexed as

Binding SitesHEK293 CellsHumansIntegrinsMolecular Docking SimulationMutationPeptide FragmentsProtein BindingProtein Conformation, alpha-HelicalProtein DomainsTalinIntegrinsPeptide FragmentsTalin

Identifiers

PMID27150043
PMCPMC4860257
OpenAlexW2339694593

What OpenQuestion holds

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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.