Evidence map›Paper›PMID 26375055›Full record

ArticleOncotarget2015

CDK1 phosphorylation of TAZ in mitosis inhibits its oncogenic activity.

Lin Zhang, Xingcheng Chen, Seth Stauffer, Shuping Yang, Yuanhong Chen, Jixin Dong

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  11. Zyxin promotes colon cancer tumorigenesis in a mitotic phosphorylation-dependent manner and through CDK8-mediated YAP activation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Review
  14. Article
  15. Regulation of TAZ in cancer.Protein & cell · 2016
    Review
  16. Article
  17. 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

6 authors at 2 institutions in 2 countries.

Lin ZhangDepartment of Radiation Oncology, Qilu Hospital of Shandong University, Jinan, Shandong, P.R. China.
Xingcheng ChenEppley Institute for Research in Cancer, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.
Seth StaufferEppley Institute for Research in Cancer, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.
Shuping YangDepartment of Oncology, Shandong Provincial Hospital affiliated with Shandong University, Jinan, Shandong, P.R. China.
Yuanhong ChenEppley Institute for Research in Cancer, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.
Jixin DongEppley Institute for Research in Cancer, Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, USA.
University of Nebraska Medical Center · USShandong Provincial Hospital · CN

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
Research Pilot Project ProgramP30GM106397 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2013 to 2017
$4.9M
Regulation and Functional Dissection of YAP in MitosisR01GM109066 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI DONG, JIXIN · 2014 to 2018
$1.4M
NCI NIH HHS P30 CA036727NIGMS NIH HHS P30 GM106397NIGMS NIH HHS R01 GM109066
6 · The paper itself

Abstract

The transcriptional co-activator with PDZ-binding motif (TAZ) is a downstream effector of the Hippo tumor suppressor pathway, which plays important roles in cancer and stem cell biology. Hippo signaling inactivates TAZ through phosphorylation (mainly at S89). In the current study, we define a new layer of regulation of TAZ activity that is critical for its oncogenic function. We found that TAZ is phosphorylated in vitro and in vivo by the mitotic kinase CDK1 at S90, S105, T326, and T346 during the G2/M phase of the cell cycle. Interestingly, mitotic phosphorylation inactivates TAZ oncogenic activity, as the non-phosphorylatable mutant (TAZ-S89A/S90A/S105A/T326A/T346A, TAZ-5A) possesses higher activity in epithelial-mesenchymal transition, anchorage-independent growth, cell migration, and invasion when compared to the TAZ-S89A mutant. Accordingly, TAZ-5A has higher transcriptional activity compared to the TAZ-S89A mutant. Finally, we show that TAZ-S89A or TAZ-5A (to a greater extent) was sufficient to induce spindle and centrosome defects, and chromosome misalignment/missegregation in immortalized epithelial cells. Together, our results reveal a previously unrecognized connection between TAZ oncogenicity and mitotic phospho-regulation.

Indexed as

AcyltransferasesBlotting, WesternCDC2 Protein KinaseCell MovementCells, CulturedCell Transformation, NeoplasticCyclin-Dependent KinasesEpithelial-Mesenchymal TransitionFluorescent Antibody TechniqueHEK293 CellsHumansImmunoenzyme TechniquesImmunoprecipitationMitosisNeoplasmsPhosphorylationAcyltransferasesCDC2 Protein KinaseCDK1 protein, humanCyclin-Dependent KinasesTAFAZZIN protein, humanTranscription FactorsCDK1Hippo pathwaymitotic defectsmitotic phosphorylationTAZ

Identifiers

PMID26375055
PMCPMC4741614
OpenAlexW2173178352

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.