Evidence map›Paper›PMID 31043565›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Cell contact and Nf2/Merlin-dependent regulation of TEAD palmitoylation and activity.

Nam-Gyun Kim, Barry M Gumbiner

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
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  3. Crosstalk between protein lipidation and ubiquitination in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
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  17. [Advances in Targeted Therapy for Malignant Pleural Mesothelioma].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2024
    Review
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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

2 authors at 2 institutions in 1 country.

Nam-Gyun KimCenter for Developmental Biology and Regenerative Medicine, Seattle Children's Research Institute, Seattle, WA 98101.
Barry M GumbinerCenter for Developmental Biology and Regenerative Medicine, Seattle Children's Research Institute, Seattle, WA 98101; gumbiner@uw.edu.
Seattle Children's Hospital · USUniversity of Washington · US

Funding

Regulation of cell junctions and cell contact dependent signaling in tissue development and physiologyR35GM122467 · NIGMS · SEATTLE CHILDREN'S HOSPITAL · PI GUMBINER, BARRY M. · 2017 to 2021
$3.9M
Cadherin Regulation of Epithelial BarriersR01GM106659 · NIGMS · UNIVERSITY OF VIRGINIA · PI GUMBINER, BARRY M. · 2013 to 2016
$1.8M
NIGMS NIH HHS R01 GM106659NIGMS NIH HHS R35 GM122467
6 · The paper itself

Abstract

The Hippo pathway is involved in regulating contact inhibition of proliferation and organ size control and responds to various physical and biochemical stimuli. It is a kinase cascade that negatively regulates the activity of cotranscription factors YAP and TAZ, which interact with DNA binding transcription factors including TEAD and activate the expression of target genes. In this study, we show that the palmitoylation of TEAD, which controls the activity and stability of TEAD proteins, is actively regulated by cell density independent of Lats, the key kinase of the Hippo pathway. The expression of fatty acid synthase and acetyl-CoA carboxylase involved in de novo biosynthesis of palmitate is reduced by cell density in an Nf2/Merlin-dependent manner. Depalmitoylation of TEAD is mediated by depalmitoylases including APT2 and ABHD17A. Palmitoylation-deficient TEAD4 mutant is unstable and degraded by proteasome through the activity of the E3 ubiquitin ligase CHIP. These findings show that TEAD activity is tightly controlled through the regulation of palmitoylation and stability via the orchestration of FASN, depalmitoylases, and E3 ubiquitin ligase in response to cell contact.

Indexed as

LipoylationDNA-Binding ProteinsFatty Acid Synthase, Type IHumansMuscle ProteinsNeurofibromin 2Nuclear ProteinsProtein Serine-Threonine KinasesTEA Domain Transcription FactorsTranscription FactorsUbiquitin-Protein LigasesDNA-Binding ProteinsFASN protein, humanFatty Acid Synthase, Type ILATS1 protein, humanMuscle ProteinsNeurofibromin 2Nuclear ProteinsProtein Serine-Threonine KinasesSTUB1 protein, humanTEAD1 protein, humanTEAD4 protein, humanTEA Domain Transcription FactorsTranscription FactorsUbiquitin-Protein Ligasesdepalmitoylasefatty acid synthaseHippo signalingpalmitoylationTEAD

Identifiers

PMID31043565
PMCPMC6525549
OpenAlexW2943492090

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.