Evidence map›Paper›PMID 11160818›Full record

ArticleMolecular biology of the cell2001

Serine phosphorylation of focal adhesion kinase in interphase and mitosis: a possible role in modulating binding to p130(Cas).

A Ma, A Richardson, E M Schaefer, J T Parsons

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Journal of biological chemistry · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. CAS proteins in normal and pathological cell growth control.Cellular and molecular life sciences : CMLS · 2010
    Review
  14. Article
  15. Review
  16. Article
  17. Integrins as regulators of the mitotic machinery.Current opinion in cell biology · 2008
    Review
  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

4 authors at 1 institution in 1 country.

A MaDepartment of Microbiology, Health Sciences Center, University of Virginia, Charlottesville, Virginia 22908, USA.
A Richardson
E M Schaefer
J T Parsons
University of Virginia · US

Funding

STRUCTURE AND FUNCTION OF A CELLULAR TYROSINE PROTEIN KINASEP01CA040042 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI MACARA, IAN G · 1985 to 2009
$10.5M
Function of Cortactin, a Src TargetR01CA029243 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PARSONS, J THOMAS · 1985 to 2005
$1.5M
AVIAN TUMOR VIRUS ANTIGENSR37CA029243 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PARSONS, J THOMAS · 1992 to 1999
–
NCI NIH HHS CA-29243NCI NIH HHS CA-40042NCI NIH HHS P01 CA040042NCI NIH HHS R01 CA029243NCI NIH HHS R37 CA029243
6 · The paper itself

Abstract

Focal adhesion kinase (FAK) is an important regulator of integrin signaling in adherent cells and accordingly its activity is significantly modulated during mitosis when cells detach from the extracellular matrix. During mitosis, FAK becomes heavily phosphorylated on serine residues concomitant with its inactivation and dephosphorylation on tyrosine. Little is known about the regulation of FAK activity by serine phosphorylation. In this report, we characterize two novel sites of serine phosphorylation within the C-terminal domain of FAK. Phosphorylation-specific antibodies directed to these sites and against two previously characterized sites of serine phosphorylation were used to study the regulated phosphorylation of FAK in unsynchronized and mitotic cells. Among the four major phosphorylation sites, designated pS1-pS4, phosphorylation of pS1 (Ser722) is unchanged in unsynchronized and mitotic cells. In contrast, pS3 and pS4 (Ser843 and Ser910) exhibit increased phosphorylation during mitosis. In vitro peptide binding experiments provide evidence that phosphorylation of pS1 (Ser722) may play a role in modulating FAK binding to the SH3 domain of the adapter protein p130(Cas).

Indexed as

Cell CycleProteinsAnimalsAntibodiesBinding, CompetitiveBinding SitesCells, CulturedChick EmbryoCrk-Associated Substrate ProteinFibroblastsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHeLa CellsHumansInterphaseMitosisAntibodiesBCAR1 protein, humanCrk-Associated Substrate ProteinFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesPhosphoproteinsProteinsProtein-Tyrosine KinasesPTK2 protein, humanRetinoblastoma-Like Protein p130Retinoblastoma ProteinSerine

Identifiers

PMID11160818
PMCPMC30563
OpenAlexW2159727608

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.