ArticleThe EMBO journal1999
A WW domain-containing yes-associated protein (YAP) is a novel transcriptional co-activator.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 285 papers.
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.
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.
Who cites it
285 citing papers in PubMed, 548 citations in OpenAlex.
- Mechanosignaling through YAP and TAZ drives fibroblast activation and fibrosis.American journal of physiology. Lung cellular and molecular physiology · 2015Trial
- Epigenetic Control of Mammalian Cardiomyocyte Proliferation.Current cardiology reports · 2026Review
- Inflammatory monocytes constrain YAP-induced cell proliferation.Science advances · 2026Article
- Tumor progression is effectively suppressed by miR-195 through direct targeting of YAP1.Frontiers in oncology · 2026Article
- Article
- YAP1 reactivation in cardiomyocytes following ECM remodelling contributes to the development of contractile force and sarcomere maturation.Cell death discovery · 2025Article
- YAP/TAZ: An epitome of tumorigenesis.Cancer letters · 2025Review
- YAP1 promotes adipogenesis by regulating the negative feedback mechanism of the Hippo signaling pathway via LATS2.Zoological research · 2025Article
- A degradable form of polyoma small T antigen reveals the high specificity of TAZ in regulating gene expression.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The mechanism of YAP/TAZ transactivation and dual targeting for cancer therapy.Nature communications · 2025Article
- Role of YAP/TAZ in bone diseases: A transductor from mechanics to biology.Journal of orthopaedic translation · 2025Review
- Stiffness Regulates the Morphology and Stemness of Limbal Niche Cells Through Unique nYAP/cYAP Translocation.Investigative ophthalmology & visual science · 2025Article
- Immunomodulatory roles of quercetin in diabetic nephropathy: targeting inflammation, oxidative stress, and ferroptosis.Frontiers in pharmacology · 2025Review
- Extracellular Vesicles Derived from Ligament Tissue Transport Interleukin-17A to Mediate Ligament-To-Bone Crosstalk in Ankylosing Spondylitis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Article
- Noncanonical functions of adhesion proteins in inflammation.American journal of physiology. Cell physiology · 2024Review
- The Impact of Molecular and Genetic Analysis on the Treatment of Patients with Atypical Meningiomas.Diagnostics (Basel, Switzerland) · 2024Review
- YAP condensates are highly organized hubs.iScience · 2024Article
- The RNF214-TEAD-YAP signaling axis promotes hepatocellular carcinoma progression via TEAD ubiquitylation.Nature communications · 2024Article
- Regulation mechanism of EBV-encoded EBER1 and LMP2A on YAP1 and the impact of YAP1 on the EBV infection status in EBV-associated gastric carcinoma.Virus research · 2024Article
225 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A protein module called the WW domain recognizes and binds to a short oligopeptide called the PY motif, PPxY, to mediate protein-protein interactions. The PY motif is present in the transcription activation domains of a wide range of transcription factors including c-Jun, AP-2, NF-E2, C/EBPalpha and PEBP2/CBF, suggesting that it plays an important role in transcriptional activation. We show here that mutation of the PY motif in the subregion of the activation domain of the DNA-binding subunit of PEBP2, PEBP2alpha, abolishes its transactivation function. Using yeast two-hybrid screening, we demonstrate that Yes-associated protein (YAP) binds to the PY motif of PEBP2alpha through its WW domain. The C-terminal region of YAP fused to the DNA-binding domain of GAL4 showed transactivation as strong as that of GAL4-VP16. Exogenously expressed YAP conferred transcription-stimulating activity on the PY motif fused to the GAL4 DNA-binding domain as well as to native PEBP2alpha. The osteocalcin promoter was stimulated by exogenous PEBP2alphaA and a dominant negative form of YAP strongly inhibited this activity, suggesting YAP involvement in this promoter activity in vivo. These results indicate that the PY motif is a novel transcription activation domain that functions by recruiting YAP as a strong transcription activator to target genes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.