ArticleProtein science : a publication of the Protein Society2018
Adaptation of the bound intrinsically disordered protein YAP to mutations at the YAP:TEAD interface.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- YAP1 and QSER1 are key modulators of embryonic signaling pathways in the mammalian epiblast.EMBO reports · 2026Article
- Article
- YAP1 and QSER1 are Key Modulators of Embryonic Signaling Pathways in the Mammalian Epiblast.bioRxiv : the preprint server for biology · 2025Article
- A Theoretical Study on the Efficacy and Mechanism of Combined YAP-1 and PARP-1 Inhibitors in the Treatment of Glioblastoma Multiforme Using Peruvian MacaCurrent issues in molecular biology · 2025Article
- Computational design and experimental confirmation of a disulfide-stapled YAP helixJournal of computer-aided molecular design · 2024Article
- Leveraging Hot Spots of TEAD-Coregulator Interactions in the Design of Direct Small Molecule Protein-Protein Interaction Disruptors Targeting Hippo Pathway Signaling.Pharmaceuticals (Basel, Switzerland) · 2023Review
- N-terminal β-strand in YAP is critical for stronger binding to scalloped relative to TEAD transcription factor.Protein science : a publication of the Protein Society · 2023Article
- Targeting the Hippo/YAP/TAZ signalling pathway: Novel opportunities for therapeutic interventions into skin cancers.Experimental dermatology · 2022Review
- The role of lysine palmitoylation/myristoylation in the function of the TEAD transcription factors.Scientific reports · 2022Article
- Review
- Article
- Article
- Study of the TEAD-binding domain of the YAP protein from animal species.Protein science : a publication of the Protein Society · 2021Article
- Matrin3: Disorder and ALS Pathogenesis.Frontiers in molecular biosciences · 2021Review
- A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors.Scientific reports · 2020Article
- Templated folding of intrinsically disordered proteins.The Journal of biological chemistry · 2020Review
- Identification of FAM181A and FAM181B as new interactors with the TEAD transcription factors.Protein science : a publication of the Protein Society · 2020Article
- YAP-dependent necrosis occurs in early stages of Alzheimer's disease and regulates mouse model pathology.Nature communications · 2020Article
- Fluorescence polarization assay for the identification and evaluation of inhibitors at YAP-TEAD protein-protein interface 3.Analytical biochemistry · 2019Article
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Authors and funding
11 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Many interactions between proteins are mediated by intrinsically disordered regions (IDRs). Intrinsically disordered proteins (IDPs) do not adopt a stable three-dimensional structure in their unbound form, but they become more structured upon binding to their partners. In this communication, we study how a bound IDR adapts to mutations, preventing the formation of hydrogen bonds at the binding interface that needs a precise positioning of the interacting residues to be formed. We use as a model the YAP:TEAD interface, where one YAP (IDP) and two TEAD residues form hydrogen bonds via their side chain. Our study shows that the conformational flexibility of bound YAP and the reorganization of water molecules at the interface help to reduce the energetic constraints created by the loss of H-bonds at the interface. The residual flexibility/dynamic of bound IDRs and water might, therefore, be a key for the adaptation of IDPs to different interface landscapes and to mutations occurring at binding interfaces.
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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.