ArticlePloS one2015
WW domains of the yes-kinase-associated-protein (YAP) transcriptional regulator behave as independent units with different binding preferences for PPxY motif-containing ligands.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 54 citations in OpenAlex.
- Comparing YAPBiomolecules · 2026Article
- Mismatch repair protein MLH1 controls testis development by regulating the Hippo-YAP signaling pathway.Nucleic acids research · 2026Article
- IQGAP Family Proteins in Colorectal Cancer: Molecular Mechanisms and Prognostic Implications.Diagnostics (Basel, Switzerland) · 2026Review
- TMEM207-mediated the impairment of skin regeneration through YAP sequestration in an allergic contact dermatitis model.Biochemistry and biophysics reports · 2026Article
- ARRDC3 promotes lysosome-mediated YAP degradation to inhibit enterovirus replication.Virologica Sinica · 2025Article
- Review
- Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs.Nature communications · 2024Article
- Nuclear phosphoinositide signaling promotes YAP/TAZ-TEAD transcriptional activity in breast cancer.The EMBO journal · 2024Article
- The landscape of alternative splicing in granulosa cells and a potential novel role of YAP1 in PCOS.PloS one · 2024Article
- Pharmacological inhibition of CLK2 activates YAP by promoting alternative splicing of AMOTL2.eLife · 2023Article
- Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex.Protein science : a publication of the Protein Society · 2022Article
- Enhanced nuclear localization of YAP1-2 contributes to EGF-induced EMT in NSCLC.Journal of cellular and molecular medicine · 2022Article
- Molecular mechanisms underlying the role of the centriolar CEP164-TTBK2 complex in ciliopathies.Structure (London, England : 1993) · 2022Article
- Screening of Yeast Display Libraries of Enzymatically Treated Peptides to Discover Macrocyclic Peptide Ligands.International journal of molecular sciences · 2021Article
- Yap1-2 Isoform Is the Primary Mediator in TGF-β1 Induced EMT in Pancreatic Cancer.Frontiers in oncology · 2021Article
- The WW domains dictate isoform-specific regulation of YAP1 stability and pancreatic cancer cell malignancy.Theranostics · 2020Article
- Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin.The Journal of biological chemistry · 2019Article
- Protein painting, an optimized MS-based technique, reveals functionally relevant interfaces of the PD-1/PD-L1 complex and the YAP2/ZO-1 complex.The Journal of biological chemistry · 2019Article
- Quantitative Analysis Reveals that Actin and Src-Family Kinases Regulate Nuclear YAP1 and Its Export.Cell systems · 2018Article
- Alternative Splicing in the Hippo Pathway-Implications for Disease and Potential Therapeutic Targets.Genes · 2018Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
YAP is a WW domain-containing effector of the Hippo tumor suppressor pathway, and the object of heightened interest as a potent oncogene and stemness factor. YAP has two major isoforms that differ in the number of WW domains they harbor. Elucidating the degree of co-operation between these WW domains is important for a full understanding of the molecular function of YAP. We present here a detailed biophysical study of the structural stability and binding properties of the two YAP WW domains aimed at investigating the relationship between both domains in terms of structural stability and partner recognition. We have carried out a calorimetric study of the structural stability of the two YAP WW domains, both isolated and in a tandem configuration, and their interaction with a set of functionally relevant ligands derived from PTCH1 and LATS kinases. We find that the two YAP WW domains behave as independent units with different binding preferences, suggesting that the presence of the second WW domain might contribute to modulate target recognition between the two YAP isoforms. Analysis of structural models and phage-display studies indicate that electrostatic interactions play a critical role in binding specificity. Together, these results are relevant to understand of YAP function and open the door to the design of highly specific ligands of interest to delineate the functional role of each WW domain in YAP signaling.
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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.