Evidence map›Paper›PMID 9396762›Full record

ArticleThe Journal of cell biology1997

Muscle beta1D integrin reinforces the cytoskeleton-matrix link: modulation of integrin adhesive function by alternative splicing.

A M Belkin, S F Retta, O Y Pletjushkina, F Balzac, L Silengo, R Fassler, V E Koteliansky, K Burridge, G Tarone

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Extracellular Matrix in Regulation of Contractile System in Cardiomyocytes.International journal of molecular sciences · 2019
    Review
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  15. Structural diversity in integrin/talin interactions.Structure (London, England : 1993) · 2010
    Article
  16. Article
  17. Analysis of conserved residues in the betapat-3 cytoplasmic tail reveals important functions of integrin in multiple tissues.Developmental dynamics : an official publication of the American Association of Anatomists · 2010
    Article
  18. Article
  19. Article
  20. 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

9 authors at 4 institutions in 3 countries.

A M BelkinDepartment of Cell Biology and Anatomy, University of North Carolina at Chapel Hill, North Carolina 27599, USA. Belkina@usa.redcross.org
S F Retta
O Y Pletjushkina
F Balzac
L Silengo
R Fassler
V E Koteliansky
K Burridge
G Tarone
University of North Carolina at Chapel Hill · USUniversity of Turin · ITMax Planck Institute of Biochemistry · DEUniversity of Palermo · IT

Funding

THE ROLE OF RAP1 IN INTEGRIN ACTIVATION AND PLATELET SIGNALINGP01HL045100 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PARISE, LESLIE V. · 1993 to 2007
$13.7M
STRUCTURE/FUNCTION OF FOCAL ADHESIONSR01GM029860 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BURRIDGE, KEITH · 1985 to 2018
$6.7M
NCI NIH HHS R29 CA72961NHLBI NIH HHS HL45100NHLBI NIH HHS P01 HL045100NIGMS NIH HHS GM29860NIGMS NIH HHS R01 GM029860Telethon 851
6 · The paper itself

Abstract

Expression of muscle-specific beta1D integrin with an alternatively spliced cytoplasmic domain in CHO and GD25, beta1 integrin-minus cells leads to their phenotypic conversion. beta1D-transfected nonmuscle cells display rounded morphology, lack of pseudopodial activity, retarded spreading, reduced migration, and significantly enhanced contractility compared with their beta1A-expressing counterparts. The transfected beta1D is targeted to focal adhesions and efficiently displaces the endogenous beta1A and alphavbeta3 integrins from the sites of cell-matrix contact. This displacement is observed on several types of extracellular matrix substrata and leads to elevated stability of focal adhesions in beta1D transfectants. Whereas a significant part of cellular beta1A integrin is extractable in digitonin, the majority of the transfected beta1D is digitonin-insoluble and is strongly associated with the detergent-insoluble cytoskeleton. Increased interaction of beta1D integrin with the actin cytoskeleton is consistent with and might be mediated by its enhanced binding to talin. In contrast, beta1A interacts more strongly with alpha-actinin, than beta1D. Inside-out driven activation of the beta1D ectodomain increases ligand binding and fibronectin matrix assembly by beta1D transfectants. Phenotypic effects of beta1D integrin expression in nonmuscle cells are due to its enhanced interactions with both cytoskeletal and extracellular ligands. They parallel the transitions that muscle cells undergo during differentiation. Modulation of beta1 integrin adhesive function by alternative splicing serves as a physiological mechanism reinforcing the cytoskeleton- matrix link in muscle cells. This reflects the major role for beta1D integrin in muscle, where extremely stable association is required for contraction.

Indexed as

Alternative SplicingCell AdhesionActinsAnimalsCell LineCHO CellsCricetinaeCytoskeletonDNA, ComplementaryExtracellular MatrixHumansIntegrin beta1Muscle ContractionMusclesMyosin Light ChainsPhosphorylationActinsDNA, ComplementaryIntegrin beta1Myosin Light ChainsReceptors, VitronectinRecombinant Fusion Proteins

Identifiers

PMID9396762
PMCPMC2132630
OpenAlexW2170820559

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.