ArticleBiochimie2014
Molecular basis of the binding of YAP transcriptional regulator to the ErbB4 receptor tyrosine kinase.
Article in Biochimie, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.
- Prognostic Value of Yes-Associated Protein 1 (YAP1) in Various Cancers: A Meta-Analysis.PloS one · 2015Pooled it
- Identification and functional comparison of novel alternatively spliced isoforms of human YAP.FEBS open bio · 2023Article
- Gone Caving: Roles of the Transcriptional Regulators YAP and TAZ in Skeletal Development.Current osteoporosis reports · 2020Review
- Endothelial YAP/TAZ Signaling in Angiogenesis and Tumor Vasculature.Frontiers in oncology · 2020Review
- 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
- Activation of ERBB4 in Glioblastoma Can Contribute to Increased Tumorigenicity and Influence Therapeutic Response.Cancers · 2018Article
- Dishevelled has a YAP nuclear export function in a tumor suppressor context-dependent manner.Nature communications · 2018Article
- DNA binding partners of YAP/TAZ.BMB reports · 2018Review
- Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction.Oncotarget · 2018Article
- FlexPepDock lessons from CAPRI peptide-protein rounds and suggested new criteria for assessment of model quality and utility.Proteins · 2017Article
- T-cell exhaustion in chronic hepatitis B infection: current knowledge and clinical significance.Cell death & disease · 2015Review
- Versatile communication strategies among tandem WW domain repeats.Experimental biology and medicine (Maywood, N.J.) · 2015Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The newly discovered transactivation function of ErbB4 receptor tyrosine kinase is believed to be mediated by virtue of the ability of its proteolytically-cleaved intracellular domain (ICD) to physically associate with YAP2 transcriptional regulator. In an effort to unearth the molecular basis of YAP2-ErbB4 interaction, we have conducted a detailed biophysical analysis of the binding of WW domains of YAP2 to PPXY motifs located within the ICD of ErbB4. Our data show that the WW1 domain of YAP2 binds to PPXY motifs within the ICD in a differential manner and that this behavior is by and large replicated by the WW2 domain. Remarkably, while both WW domains absolutely require the integrity of the PPXY consensus sequence, non-consensus residues within and flanking this motif do not appear to be critical for binding. In spite of this shared mode of binding, the WW domains of YAP2 display distinct conformational dynamics in complex with PPXY motifs derived from ErbB4. Collectively, our study lends new insights into the molecular basis of a key protein-protein interaction involved in a diverse array of cellular processes.
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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.