Evidence map›Paper›PMID 25694433›Full record

ArticleThe Journal of biological chemistry2015

Direct interactions with the integrin β1 cytoplasmic tail activate the Abl2/Arg kinase.

Mark A Simpson, William D Bradley, David Harburger, Maddy Parsons, David A Calderwood, Anthony J Koleske

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Use of Ecto-Tagged Integrins to Monitor Integrin Exocytosis and Endocytosis.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Article
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  9. Review
  10. Abl2:Cortactin Interactions Regulate Dendritic Spine Stability via Control of a Stable Filamentous Actin Pool.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  11. Review
  12. Article
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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

6 authors at 2 institutions in 2 countries.

Mark A SimpsonFrom the Departments of Molecular Biophysics and Biochemistry.
William D BradleyFrom the Departments of Molecular Biophysics and Biochemistry.
David HarburgerPharmacology.
Maddy Parsonsthe Randall Division of Cell and Molecular Biophysics, Kings College, London WC2R 2LS, United Kingdom.
David A CalderwoodPharmacology, Cell Biology, and.
Anthony J KoleskeFrom the Departments of Molecular Biophysics and Biochemistry, Neurobiology, Yale University, New Haven, Connecticut 06510 and anthony.koleske@yale.edu.
Yale University · USKing's College London · GB

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Integrin-Filamin Interactions in Migration and SignalingR01GM068600 · NIGMS · YALE UNIVERSITY · PI CALDERWOOD, DAVID A · 2003 to 2016
$4.4M
Supplement to Regulation of invadopodia formation in breast cancer cellsR01CA133346 · NCI · YALE UNIVERSITY · PI KOLESKE, ANTHONY J · 2009 to 2016
$2.3M
Laminin control of CNS dendrite and dendritic spine developmentR01NS089662 · NINDS · YALE UNIVERSITY · PI GRUTZENDLER, JAIME, KOLESKE, ANTHONY J · 2014 to 2018
$1.8M
The mechanism of Arg kinase activation by integrin B1R01GM100411 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, KOLESKE, ANTHONY J · 2012 to 2015
$1.3M
NCI NIH HHS CA133346NCI NIH HHS R01 CA133346NIGMS NIH HHS GM100411NIGMS NIH HHS R01 GM068600NIGMS NIH HHS R01 GM100411NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32GM007223-40NINDS NIH HHS R01 NS089662
6 · The paper itself

Abstract

Integrins are heterodimeric α/β extracellular matrix adhesion receptors that couple physically to the actin cytoskeleton and regulate kinase signaling pathways to control cytoskeletal remodeling and adhesion complex formation and disassembly. β1 integrins signal through the Abl2/Arg (Abl-related gene) nonreceptor tyrosine kinase to control fibroblast cell motility, neuronal dendrite morphogenesis and stability, and cancer cell invasiveness, but the molecular mechanisms by which integrin β1 activates Arg are unknown. We report here that the Arg kinase domain interacts directly with a lysine-rich membrane-proximal segment in the integrin β1 cytoplasmic tail, that Arg phosphorylates the membrane-proximal Tyr-783 in the β1 tail, and that the Arg Src homology domain then engages this phosphorylated region in the tail. We show that these interactions mediate direct binding between integrin β1 and Arg in vitro and in cells and activate Arg kinase activity. These findings provide a model for understanding how β1-containing integrins interact with and activate Abl family kinases.

Indexed as

Amino Acid SequenceCatalytic DomainEnzyme ActivationHEK293 CellsHumansIntegrin beta1Molecular Sequence DataPhosphorylationProtein Interaction Domains and MotifsProtein Interaction MappingProtein Processing, Post-TranslationalProtein-Tyrosine KinasesARG tyrosine kinaseIntegrin beta1Protein-Tyrosine KinasesAbl Tyrosine KinaseIntegrinPhosphorylationProtein-Protein InteractionSrc Homology 2 Domain (SH2 Domain)

Identifiers

PMID25694433
PMCPMC4375489
OpenAlexW2020325784

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.