Evidence map›Paper›PMID 1385444›Full record

ArticleThe Journal of cell biology1992

Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly.

K Burridge, C E Turner, L H Romer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 364 papers.

0numbers the graph read from it
0cells of the map it votes in
364citing papers in PubMed
25.3field-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

364 citing papers in PubMed, 1,316 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Reduced cell-substrate adhesion formation promotes cell migration inbioRxiv : the preprint server for biology · 2025
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  20. Review

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

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.

K BurridgeDepartment of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599.
C E Turner
L H Romer
University of North Carolina at Chapel Hill · US

Funding

STRUCTURE/FUNCTION OF FOCAL ADHESIONSR01GM029860 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BURRIDGE, KEITH · 1985 to 2018
$6.7M
STRUCTURE AND FUNCTION OF PAXILLINR01GM047607 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI TURNER, CHRISTOPHER E · 1996 to 2017
$5.5M
INTEGRIN-CYTOSKELETAL INTERACTIONS IN PLATELETSR01HL044918 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI BURRIDGE, KEITH · 1991 to 1992
–
STRUCTURE AND FUNCTION OF PAXILLINR29GM047607 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI TURNER, CHRISTOPHER E · 1991 to 1995
–
NHLBI NIH HHS HL-44918NIGMS NIH HHS GM-29860NIGMS NIH HHS GM-47607
6 · The paper itself

Abstract

Cells in culture reveal high levels of protein tyrosine phosphorylation in their focal adhesions, the regions where cells adhere to the underlying substratum. We have examined the tyrosine phosphorylation of proteins in response to plating cells on extracellular matrix substrata. Rat embryo fibroblasts, mouse Balb/c 3T3, and NIH 3T3 cells plated on fibronectin-coated surfaces revealed elevated phosphotyrosine levels in a cluster of proteins between 115 and 130 kD. This increase in tyrosine phosphorylation was also seen when rat embryo fibroblasts were plated on laminin or vitronectin, but not on polylysine or on uncoated plastic. Integrin mediation of this effect was suggested by finding the same pattern of elevated tyrosine phosphorylation in cells plated on the cell-binding fragment of fibronectin and in cells plated on a synthetic polymer containing multiple RGD sequences. We have identified one of the proteins of the 115-130-kD cluster as pp125FAK, a tyrosine kinase recently localized in focal adhesions (Schaller, M. D., C. A. Borgman, B. S. Cobb, R. R. Vines, A. B. Reynolds, and J. T. Parsons. 1992. Proc. Natl. Acad. Sci. USA. 89:5192). A second protein that becomes tyrosine phosphorylated in response to extracellular matrix adhesion is identified as paxillin, a 70-kD protein previously localized to focal adhesions. Treatment of cells with the tyrosine kinase inhibitor herbimycin A diminished the adhesion-induced tyrosine phosphorylation of these proteins and inhibited the formation of focal adhesions and stress fibers. These results suggest a role for integrin-mediated tyrosine phosphorylation in the organization of the cytoskeleton as cells adhere to the extracellular matrix.

Indexed as

Cell Adhesion3T3 CellsAnimalsBenzoquinonesBlotting, WesternCell Adhesion MoleculesCell LineCytoskeletal ProteinsExtracellular MatrixFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesIntegrinsLactams, MacrocyclicMicePaxillinBenzoquinonesCell Adhesion MoleculesCytoskeletal ProteinsFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesherbimycinIntegrinsLactams, MacrocyclicPaxillinPhosphoproteinsPhosphotyrosineProtein-Tyrosine KinasesPtk2 protein, mousePtk2 protein, ratPxn protein, mousePxn protein, ratQuinonesRifabutinTyrosine

Identifiers

PMID1385444
PMCPMC2289706
OpenAlexW2148849095

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.