Evidence map›Paper›PMID 31422909›Full record

ArticleStructure (London, England : 1993)2019

Distinct Binding Modes of Vinculin Isoforms Underlie Their Functional Differences.

Andrey Krokhotin, Muzaddid Sarker, Ernesto Alva Sevilla, Lindsey M Costantini, Jack D Griffith, Sharon L Campbell, Nikolay V Dokholyan

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 2 institutions in 2 countries.

Andrey KrokhotinDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Departments of Pathology, Genetics and Developmental Biology, Howard Hughes Medical Institute, Stanford Medical School, Palo Alto, CA 94305, USA.
Muzaddid SarkerDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
Ernesto Alva SevillaDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Lindsey M CostantiniDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Jack D GriffithDepartment of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Sharon L CampbellDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. Electronic address: campbesl@med.unc.edu.
Nikolay V DokholyanDepartment of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA; Departments of Pharmacology and Departments of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA 17033, USA. Electronic address: dokh@psu.edu.
University of North Carolina at Chapel Hill · USUniversity of Ottawa · CA

Funding

Vironomics and Biostatistics CoreP01CA019014 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BLOSSOM A DAMANIA, NANCY JOAN RAAB-TRAUB · 1985 to 2026
$43.8M
UTSA RISE Research Training ProgramR25GM060655 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI BAREA-RODRIGUEZ, EDWIN J · 2000 to 2022
$21.6M
HOMOLOOUS RECOMBINATION: ITS MOLECULAR CYTOLOGYR01GM031819 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 1985 to 2017
$5.2M
Structure and Mechanism of G-proteins and cell adhesion proteins in regulation of cell growth and motilityR35GM134962 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Sharon L Campbell · 2020 to 2026
$4.2M
Nucleoprotein structures formed at sites of DNA damageR01ES013773 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 2005 to 2015
$3.2M
Mechanisms of vinculin activation and force transmissionR01GM115597 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CAMPBELL, SHARON L · 2016 to 2019
$1.6M
Engineering allostery for in vivo protein controlR01GM123247 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOKHOLYAN, NIKOLAY · 2017 to 2019
$1.5M
Integrating cheminformatics and molecular simulations for virtual drug screeningR01GM114015 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOKHOLYAN, NIKOLAY · 2016 to 2019
$1.1M
The structure of the telomere as a sentinel of DNA damage.R56ES013773 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 2019 to 2019
$150k
NCI NIH HHS P01 CA019014NIEHS NIH HHS R01 ES013773NIEHS NIH HHS R56 ES013773NIGMS NIH HHS R01 GM031819NIGMS NIH HHS R01 GM114015NIGMS NIH HHS R01 GM115597NIGMS NIH HHS R01 GM123247NIGMS NIH HHS R25 GM060655NIGMS NIH HHS R35 GM134962
6 · The paper itself

Abstract

Vinculin and its splice isoform metavinculin play key roles in regulating cellular morphology, motility, and force transduction. Vinculin is distinct from metavinculin in its ability to bundle filamentous actin (F-actin). To elucidate the molecular basis for these differences, we employed computational and experimental approaches. Results from these analyses suggest that the C terminus of both vinculin and metavinculin form stable interactions with the F-actin surface. However, the metavinculin tail (MVt) domain contains a 68 amino acid insert, with helix 1 (H1) sequestered into a globular subdomain, which protrudes from the F-actin surface and prevents actin bundling by sterically occluding actin filaments. Consistent with our model, deletion and selective point mutations within the MVt H1 disrupt this protruding structure, and facilitate actin bundling similar to vinculin tail (Vt) domain.

Indexed as

ActinsAlternative SplicingAnimalsBinding SitesCryoelectron MicroscopyModels, MolecularMutationProtein BindingProtein DomainsProtein Structure, SecondaryVinculinActinsmetavinculinVinculinactincardiomyopathyheartmetavinculinmolecular dynamicsvinculin

Identifiers

PMID31422909
PMCPMC6774862
OpenAlexW2967755379

What OpenQuestion holds

Textmetadata
LicenceTDM
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.