Evidence map›Paper›PMID 17178732›Full record

ArticleThe Journal of biological chemistry2007

Caspase proteolysis of the integrin beta4 subunit disrupts hemidesmosome assembly, promotes apoptosis, and inhibits cell migration.

Michael E Werner, Feng Chen, Jose V Moyano, Fruma Yehiely, Jonathan C R Jones, Vincent L Cryns

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Clinical significance of the integrin α6β4 in human malignancies.Laboratory investigation; a journal of technical methods and pathology · 2015
    Review
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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 1 institution in 1 country.

Michael E WernerCell Death Regulation Laboratory, Department of Medicine, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Feng Chen
Jose V Moyano
Fruma Yehiely
Jonathan C R Jones
Vincent L Cryns
Northwestern University · US

Funding

SPORE IN BREAST CANCERP50CA089018 · NCI · NORTHWESTERN UNIVERSITY · PI JORDAN, VIRGIL CRAIG · 2000 to 2004
$14.2M
TRAINING IN METABOLISM, DIABETES AND ENDOCRINOLOGYT32DK007169 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Joseph Bass · 1988 to 2026
$6.6M
Keratinocyte Migration and Wound HealingR01AR054184 · NIAMS · WASHINGTON STATE UNIVERSITY · PI JONES, JONATHAN C. · 2006 to 2015
$3.3M
Role of alphaB-Crystallin in Cancer Cell DeathR01CA097198 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CRYNS, VINCENT L. · 2003 to 2007
$1.0M
NCI NIH HHS P50 CA089018NCI NIH HHS P50CA89018NCI NIH HHS R01 CA097198NCI NIH HHS R01CA097198NIAMS NIH HHS R01 AR054184NIAMS NIH HHS R01AR054184NIDDK NIH HHS T32 DK007169NIDDK NIH HHS T32DK07169
6 · The paper itself

Abstract

Caspases are a conserved family of cell death proteases that cleave intracellular substrates at Asp residues to modify their function and promote apoptosis. In this report we identify the integrin beta4 subunit as a novel caspase substrate using an expression cloning strategy. Together with its alpha6 partner, alpha6beta4 integrin anchors epithelial cells to the basement membrane at specialized adhesive structures known as hemidesmosomes and plays a critical role in diverse epithelial cell functions including cell survival and migration. We show that integrin beta4 is cleaved by caspase-3 and -7 at a conserved Asp residue (Asp(1109)) in vitro and in epithelial cells undergoing apoptosis, resulting in the removal of most of its cytoplasmic tail. Caspase cleavage of integrin beta4 produces two products, 1) a carboxyl-terminal product that is unstable and rapidly degraded by the proteasome and 2) an amino-terminal cleavage product (amino acids 1-1109) that is unable to assemble into mature hemidesmosomes. We also demonstrate that caspase cleavage of integrin beta4 sensitizes epithelial cells to apoptosis and inhibits cell migration. Taken together, we have identified a previously unrecognized proteolytic truncation of integrin beta4 generated by caspases that disrupts key structural and functional properties of epithelial cells and promotes apoptosis.

Indexed as

ApoptosisCaspase 3Caspase 7Cell AdhesionCell Line, TumorCell MovementCell SurvivalEpithelial CellsHemidesmosomesHumansIntegrin alpha6beta4Integrin beta4Proteasome Endopeptidase ComplexCaspase 3Caspase 7Integrin alpha6beta4Integrin beta4Proteasome Endopeptidase Complex

Identifiers

PMID17178732
PMCPMC2819670
OpenAlexW1980166997

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.