Evidence map›Paper›PMID 21994943›Full record

ArticleThe Journal of biological chemistry2011

Cellular settings mediating Src Substrate switching between focal adhesion kinase tyrosine 861 and CUB-domain-containing protein 1 (CDCP1) tyrosine 734.

Andreas Wortmann, Yaowu He, Melinda E Christensen, MayLa Linn, John W Lumley, Pamela M Pollock, Nigel J Waterhouse, John D Hooper

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact, top 97% 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

25 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
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  6. Loss of CDCP1 triggers FAK activation in detached prostate cancer cells.American journal of clinical and experimental urology · 2021
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  12. CD318 is a ligand for CD6.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Pyk2 phosphorylation of VE-PTP downstream of STIM1-induced CaAmerican journal of physiology. Lung cellular and molecular physiology · 2017
    Article
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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

8 authors at 3 institutions in 1 country.

Andreas WortmannMater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, Queensland 4101; Institute of Health and Biomedical Innovation, Queensland University of Technology, Kelvin Grove, Queensland 4059.
Yaowu HeMater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, Queensland 4101.
Melinda E ChristensenMater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, Queensland 4101.
MayLa LinnInstitute of Health and Biomedical Innovation, Queensland University of Technology, Kelvin Grove, Queensland 4059.
John W LumleyWesley Medical Centre, Auchenflower, Queensland 4066, Australia.
Pamela M PollockInstitute of Health and Biomedical Innovation, Queensland University of Technology, Kelvin Grove, Queensland 4059.
Nigel J WaterhouseMater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, Queensland 4101.
John D HooperMater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, Queensland 4101. Electronic address: jhooper@mmri.mater.org.au.
Mater Research · AUQueensland University of Technology · AUWesley Hospital · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reciprocal interactions between Src family kinases (SFKs) and focal adhesion kinase (FAK) are critical during changes in cell attachment. Recently it has been recognized that another SFK substrate, CUB-domain-containing protein 1 (CDCP1), is differentially phosphorylated during these events. However, the molecular processes underlying SFK-mediated phosphorylation of CDCP1 are poorly understood. Here we identify a novel mechanism in which FAK tyrosine 861 and CDCP1-Tyr-734 compete as SFK substrates and demonstrate cellular settings in which SFKs switch between these sites. Our results show that stable CDCP1 expression induces robust SFK-mediated phosphorylation of CDCP1-Tyr-734 with concomitant loss of p-FAK-Tyr-861 in adherent HeLa cells. SFK substrate switching in these cells is dependent on the level of expression of CDCP1 and is also dependent on CDCP1-Tyr-734 but is independent of CDCP1-Tyr-743 and -Tyr-762. In HeLa CDCP1 cells, engagement of SFKs with CDCP1 is accompanied by an increase in phosphorylation of Src-Tyr-416 and a change in cell morphology to a fibroblastic appearance dependent on CDCP1-Tyr-734. SFK switching between FAK-Tyr-861 and CDCP1-Tyr-734 also occurs during changes in adhesion of colorectal cancer cell lines endogenously expressing these two proteins. Consistently, increased p-FAK-Tyr-861 levels and a more epithelial morphology are seen in colon cancer SW480 cells silenced for CDCP1. Unlike protein kinase Cδ, FAK does not appear to form a trimeric complex with Src and CDCP1. These data demonstrate novel aspects of the dynamics of SFK-mediated cell signaling that may be relevant during cancer progression.

Indexed as

Antigens, CDAntigens, NeoplasmBinding SitesCell AdhesionCell Adhesion MoleculesCell Line, TumorCell MembraneDisease ProgressionFibroblastsFocal Adhesion Protein-Tyrosine KinasesGene SilencingHeLa CellsHumansMicroscopy, ConfocalNeoplasm ProteinsPhosphorylationAntigens, CDAntigens, NeoplasmCDCP1 protein, humanCell Adhesion MoleculesFocal Adhesion Protein-Tyrosine KinasesNeoplasm Proteinssrc-Family KinasesTyrosine

Identifiers

PMID21994943
PMCPMC3234987
OpenAlexW1498129657

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.