Evidence map›Paper›PMID 1725602›Full record

ArticleCell regulation1991

Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein.

J L Guan, J E Trevithick, R O Hynes

Abstract read
In one paragraph

Article in Cell regulation, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers.

0numbers the graph read from it
0cells of the map it votes in
177citing papers in PubMed
12.2field-weighted citation impact, top 1% 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

177 citing papers in PubMed, 571 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. FAK: A Potential Target for Cancer Therapy.ACS medicinal chemistry letters · 2025
    Article
  5. Focal adhesion kinase-mediated interaction between tumor and immune cells in the tumor microenvironment: implications for cancer-associated therapies and tumor progression.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Development of FAK Inhibitors: A Five-Year Update.International journal of molecular sciences · 2022
    Review
  12. Article
  13. FAK in Cancer: From Mechanisms to Therapeutic Strategies.International journal of molecular sciences · 2022
    Review
  14. Article
  15. Article
  16. 7-Biomolecules · 2019
    Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

J L GuanDepartment of Biology, Massachusetts Institute of Technology, Cambridge 02139.
J E Trevithick
R O Hynes
Massachusetts Institute of Technology · US

Funding

CELL-SURFACE STRUCTURE AND TRANSFORMATIONSR01CA017007 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HYNES, RICHARD O · 1985 to 2005
$2.9M
STRUCTURE-FUNCTION RELATIONSHIPS OF FIBRONECTINP01CA026712 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HYNES, RICHARD O · 1985 to 1991
–
NCI NIH HHS P01CA26712NCI NIH HHS R01CA17007
6 · The paper itself

Abstract

We describe a 120-kDa protein (pp120) that is phosphorylated on tyrosine in cells attached to fibronectin-coated surfaces. The protein appears to be located in focal contacts where it codistributes with beta 1 integrins. pp120 is distinct from the beta 1 subunit of integrins and from vinculin and alpha-actinin. pp120 is rapidly dephosphorylated in cells suspended by trypsinization but becomes rapidly phosphorylated in cells attaching and spreading on fibronectin. Attachment of cells to RGD-containing peptides, polylysine, or concanavalin A is not sufficient to induce phosphorylation of pp120. The 120-kDa cell-binding domain of fibronectin can induce some phosphorylation of pp120, but further phosphorylation occurs in the presence also of the heparin-binding domain of fibronectin. Phosphorylation of pp120 precedes, but is correlated with, subsequent cell spreading. Phosphorylation of pp120 can also be triggered by attachment of cells to anti-integrin antibodies, and this requires the cytoplasmic domain of the integrin beta 1 subunit. Thus interaction of beta 1 integrins with extracellular ligands (fibronectin or antibodies) triggers phosphorylation of an intracellular 120-kDa protein, pp120, that may be involved in the responses of cells to attachment.

Indexed as

Cell Adhesion3T3 CellsAnimalsFibronectinsFluorescent Antibody TechniqueIntegrinsMiceMolecular WeightPeptide FragmentsPhosphoproteinsPhosphorylationPhosphotyrosineProtein BindingSignal TransductionTime FactorsTyrosineFibronectinsIntegrinsPeptide FragmentsPhosphoproteinsPhosphotyrosineTyrosine

Identifiers

PMID1725602
PMCPMC361893
OpenAlexW2108674983

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.