Evidence map›Paper›PMID 18227151›Full record

ArticleMolecular and cellular biology2008

TAZ promotes cell proliferation and epithelial-mesenchymal transition and is inhibited by the hippo pathway.

Qun-Ying Lei, Heng Zhang, Bin Zhao, Zheng-Yu Zha, Feng Bai, Xin-Hai Pei, Shimin Zhao, Yue Xiong, Kun-Liang Guan

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 588 papers.

0numbers the graph read from it
0cells of the map it votes in
588citing papers in PubMed
12.5field-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

588 citing papers in PubMed, 916 citations in OpenAlex.

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  14. A proteome-wide dependency map of protein interaction motifs.Nature structural & molecular biology · 2026
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528 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

9 authors at 3 institutions in 2 countries.

Qun-Ying LeiDepartment of Biological Chemistry, School of Medicine, Molecular and Cellular Biology Laboratory, Institutes of Biomedical Sciences, Department of Biology, School of Life Science, Fudan University, Shanghai 200032, China. qlei@fudan.edu.cn
Heng Zhang
Bin Zhao
Zheng-Yu Zha
Feng Bai
Xin-Hai Pei
Shimin Zhao
Yue Xiong
Kun-Liang Guan
Fudan University · CNUniversity of North Carolina at Chapel Hill · USUniversity of California, San Diego · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TAZ is a WW domain containing a transcription coactivator that modulates mesenchymal differentiation and development of multiple organs. In this study, we show that TAZ is phosphorylated by the Lats tumor suppressor kinase, a key component of the Hippo pathway, whose alterations result in organ and tissue hypertrophy in Drosophila and contribute to tumorigenesis in humans. Lats phosphorylates TAZ on several serine residues in the conserved HXRXXS motif and creates 14-3-3 binding sites, leading to cytoplasmic retention and functional inactivation of TAZ. Ectopic expression of TAZ stimulates cell proliferation, reduces cell contact inhibition, and promotes epithelial-mesenchymal transition (EMT). Elimination of the Lats phosphorylation sites results in a constitutively active TAZ, enhancing the activity of TAZ in promoting cell proliferation and EMT. Our results elucidate a molecular mechanism for TAZ regulation and indicate a potential function of TAZ as an important target of the Hippo pathway in regulating cell proliferation tumorigenesis.

Indexed as

14-3-3 ProteinsAcyltransferasesAmino Acid MotifsCell Cycle ProteinsCell DivisionCell Line, TumorCell MovementCell TransdifferentiationCell Transformation, Neoplasticc-Mer Tyrosine KinaseConserved SequenceDrosophila ProteinsEpithelial CellsHippo KinasesHumansMembrane Proteins14-3-3 ProteinsAcyltransferasesCell Cycle Proteinsc-Mer Tyrosine KinaseDrosophila Proteinsex protein, DrosophilaHippo KinasesMembrane ProteinsMERTK protein, humanNerve Tissue ProteinsNuclear ProteinsProteinsProtein Serine-Threonine KinasesProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesRecombinant Fusion ProteinsSAV1 protein, humanSerine-Threonine Kinase 3SGMS1 protein, humanSTK3 protein, humanTAFAZZIN protein, humanTranscription FactorsTransferases (Other Substituted Phosphate Groups)YY1AP1 protein, human

Identifiers

PMID18227151
PMCPMC2268418
OpenAlexW2135726634

What Socratic 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 Socratic graph.