Evidence map›Paper›PMID 7556090›Full record

ArticleThe EMBO journal1995

Signal transduction by the alpha 6 beta 4 integrin: distinct beta 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes.

F Mainiero, A Pepe, K K Wary, L Spinardi, M Mohammadi, J Schlessinger, F G Giancotti

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 239 citations in OpenAlex.

  1. Structure, function and usage of integrin alpha 6 (CD49f): A comprehensive review.Biomedical papers of the Medical Faculty of the University Palacky, Olomouc, Czechoslovakia · 2026
    Review
  2. Review
  3. Review
  4. Mechanical regulation of signal transduction in angiogenesis.Frontiers in cell and developmental biology · 2022
    Review
  5. Article
  6. Article
  7. Insights into the Shc Family of Adaptor Proteins.Journal of molecular signaling · 2017
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

F MainieroDepartment of Pathology, Kaplan Comprehensive Cancer Center, New York University School of Medicine, NY 10016, USA.
A Pepe
K K Wary
L Spinardi
M Mohammadi
J Schlessinger
F G Giancotti
New York University · USVita-Salute San Raffaele University · IT

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
MOLECULAR ANALYSIS OF THE ALPHA6-BETA4 INTEGRINR01CA058976 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI GIANCOTTI, FILIPPO G · 1994 to 2002
$892k
NCI NIH HHS P30-CA16087NCI NIH HHS R01-CA58976
6 · The paper itself

Abstract

We have examined the mechanism of signal transduction by the hemidesmosomal integrin alpha 6 beta 4, a laminin receptor involved in morphogenesis and tumor progression. Immunoprecipitation and immune complex kinase assays indicated that antibody- or laminin-induced ligation of alpha 6 beta 4 causes tyrosine phosphorylation of the beta 4 subunit in intact cells and that this event is mediated by a protein kinase(s) physically associated with the integrin. Co-immunoprecipitation and GST fusion protein binding experiments showed that the adaptor protein Shc forms a complex with the tyrosine-phosphorylated beta 4 subunit. Shc is then phosphorylated on tyrosine residues and recruits the adaptor Grb2, thereby potentially linking alpha 6 beta 4 to the ras pathway. The beta 4 subunit was found to be phosphorylated at multiple tyrosine residues in vivo, including a tyrosine-based activation motif (TAM) resembling those found in T and B cell receptors. Phenylalanine substitutions at the beta 4 TAM disrupted association of alpha 6 beta 4 with hemidesmosomes, but did not interfere with tyrosine phosphorylation of Shc and recruitment of Grb2. These results indicate that signal transduction by the alpha 6 beta 4 integrin is mediated by an associated tyrosine kinase and that phosphorylation of distinct sites in the beta 4 tail mediates assembly of the hemidesmosomal cytoskeleton and recruitment of Shc/Grb2.

Indexed as

Adaptor Proteins, Signal TransducingSignal TransductionAmino Acid SequenceAnimalsAntigens, CDAntigens, NeoplasmAntigens, SurfaceCell AdhesionCell Adhesion MoleculesCytoskeletonDesmosomesDNA Mutational AnalysisFluorescent Antibody TechniqueGRB2 Adaptor ProteinHumansIntegrin alpha6beta4Adaptor Proteins, Signal TransducingAntigens, CDAntigens, NeoplasmAntigens, SurfaceCell Adhesion MoleculesGRB2 Adaptor ProteinGRB2 protein, humanGrb2 protein, ratIntegrin alpha6beta4Integrin beta4IntegrinsKalininProteinsProtein-Tyrosine KinasesRecombinant Proteins

Identifiers

PMID7556090
PMCPMC394539
OpenAlexW1810163104

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.