Evidence map›Paper›PMID 9658172›Full record

ArticleMolecular biology of the cell1998

Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin.

M C Brown, J A Perrotta, C E Turner

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.9field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
  2. Reduced cell-substrate adhesion formation promotes cell migration inbioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Hsp27 inhibits sublethal, Src-mediated renal epithelial cell injury.American journal of physiology. Renal physiology · 2009
    Article
  15. Article
  16. Article
  17. Article
  18. Paxillin comes of age.Journal of cell science · 2008
    Review
  19. Halothane affects focal adhesion proteins in the A 549 cells.Molecular and cellular biochemistry · 2007
    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

3 authors at 1 institution in 1 country.

M C BrownDepartment of Anatomy and Cell Biology, Program in Cell and Molecular Biology, State University of New York Health Science Center at Syracuse, Syracuse, New York 13210, USA.
J A Perrotta
C E Turner
State University of New York · US

Funding

STRUCTURE AND FUNCTION OF PAXILLINR01GM047607 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI TURNER, CHRISTOPHER E · 1996 to 2017
$5.5M
STRUCTURE AND FUNCTION OF PAXILLINR29GM047607 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI TURNER, CHRISTOPHER E · 1991 to 1995
–
NIGMS NIH HHS GM-47607NIGMS NIH HHS R01 GM047607
6 · The paper itself

Abstract

We have previously shown that the LIM domains of paxillin operate as the focal adhesion (FA)-targeting motif of this protein. In the current study, we have identified the capacity of paxillin LIM2 and LIM3 to serve as binding sites for, and substrates of serine/threonine kinases. The activities of the LIM2- and LIM3-associated kinases were stimulated after adhesion of CHO.K1 cells to fibronectin; consequently, a role for LIM domain phosphorylation in regulating the subcellular localization of paxillin after adhesion to fibronectin was investigated. An avian paxillin-CHO.K1 model system was used to explore the role of paxillin phosphorylation in paxillin localization to FAs. We found that mutations of paxillin that mimicked LIM domain phosphorylation accelerated fibronectin-induced localization of paxillin to focal contacts. Further, blocking phosphorylation of the LIM domains reduced cell adhesion to fibronectin, whereas constitutive LIM domain phosphorylation significantly increased the capacity of cells to adhere to fibronectin. The potentiation of FA targeting and cell adhesion to fibronectin was specific to LIM domain phosphorylation as mutation of the amino-terminal tyrosine and serine residues of paxillin that are phosphorylated in response to fibronectin adhesion had no effect on the rate of FA localization or cell adhesion. This represents the first demonstration of the regulation of protein localization through LIM domain phosphorylation and suggests a novel mechanism of regulating LIM domain function. Additionally, these results provide the first evidence that paxillin contributes to "inside-out" integrin-mediated signal transduction.

Indexed as

Amino Acid SequenceAnimalsCell AdhesionCHO CellsClone CellsCricetinaeCytoskeletal ProteinsDNA Mutational AnalysisFibroblastsFibronectinsMolecular Sequence DataMutagenesis, Site-DirectedPaxillinPeptide FragmentsPhosphoproteinsPhosphorylationCytoskeletal ProteinsFibronectinsPaxillinPeptide FragmentsPhosphoproteinsRecombinant Fusion ProteinsSerineThreonine

Identifiers

PMID9658172
PMCPMC25420
OpenAlexW2022541364

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.