Evidence map›Paper›PMID 9585424›Full record

ArticleThe Journal of cell biology1998

Modulation of integrin activity is vital for morphogenesis.

M D Martin-Bermudo, O M Dunin-Borkowski, N H Brown

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. LanB1 Cooperates With Kon-Tiki During Embryonic Muscle Migration inFrontiers in cell and developmental biology · 2021
    Article
  4. Article
  5. Article
  6. Zasp regulates integrin activation.Journal of cell science · 2012
    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

3 authors at 1 institution in 1 country.

M D Martin-BermudoWellcome/CRC Institute, Cambridge CB2 1QR, England; and Department of Biochemistry, Cambridge University, Cambridge CB2 1QW, England.
O M Dunin-Borkowski
N H Brown
University of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells can vary their adhesive properties by modulating the affinity of integrin receptors. The activation and inactivation of integrins by inside-out mechanisms acting on the cytoplasmic domains of the integrin subunits has been demonstrated in platelets, lymphocytes, and keratinocytes. We show that in the embryo, normal morphogenesis requires the alpha subunit cytoplasmic domain to control integrin adhesion at the right times and places. PS2 integrin (alphaPS2betaPS) adhesion is normally restricted to the muscle termini, where it is required for attaching the muscles to the ends of other muscles and to specialized epidermal cells. Replacing the wild-type alphaPS2 with mutant forms containing cytoplasmic domain deletions results in the rescue of the majority of defects associated with the absence of the alphaPS2 subunit, however, the mutant PS2 integrins are excessively active. Muscles containing these mutant integrins make extra muscle attachments at aberrant positions on the muscle surface, disrupting the muscle pattern and causing embryonic lethality. A gain- of-function phenotype is not observed in the visceral mesoderm, showing that regulation of integrin activity is tissue-specific. These results suggest that the alphaPS2 subunit cytoplasmic domain is required for inside-out regulation of integrin affinity, as has been seen with the integrin alphaIIbbeta3.

Indexed as

Drosophila ProteinsAmino Acid SequenceAnimalsConserved SequenceCytoplasmDNA PrimersDrosophilaEmbryo, NonmammalianExonsGenes, LethalIntegrin alpha ChainsIntegrinsMacromolecular SubstancesMolecular Sequence DataMorphogenesisMutagenesis, Site-DirectedDNA PrimersDrosophila Proteinsif protein, DrosophilaIntegrin alpha ChainsIntegrinsMacromolecular Substances

Identifiers

PMID9585424
PMCPMC2132760
OpenAlexW2082328100

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.