ArticleBiochemistry2013
Molecular origin of the binding of WWOX tumor suppressor to ErbB4 receptor tyrosine kinase.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- The Yin and Yang of ERBB4: Tumor Suppressor and Oncoprotein.Pharmacological reviews · 2022Review
- Neurological Disorders Associated with WWOX Germline Mutations-A Comprehensive Overview.Cells · 2021Review
- Aberrations of Chromosomes 1 and 16 in Breast Cancer: A Framework for Cooperation of Transcriptionally Dysregulated Genes.Cancers · 2021Article
- 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
- Expression of B Cell-Specific Moloney Murine Leukemia Virus Integration Site 1 (BMI-1) and WW Domain-Containing Oxidoreductase (WWOX) in Liver Cancer Tissue and Normal Liver Tissue.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- Delineating WWOX Protein Interactome by Tandem Affinity Purification-Mass Spectrometry: Identification of Top Interactors and Key Metabolic Pathways Involved.Frontiers in oncology · 2018Article
- Review
- FlexPepDock lessons from CAPRI peptide-protein rounds and suggested new criteria for assessment of model quality and utility.Proteins · 2017Article
- Fhit and Wwox loss-associated genome instability: A genome caretaker one-two punch.Advances in biological regulation · 2017Article
- Pleiotropic Functions of Tumor Suppressor WWOX in Normal and Cancer Cells.The Journal of biological chemistry · 2015Review
- Allostery mediates ligand binding to WWOX tumor suppressor via a conformational switch.Journal of molecular recognition : JMR · 2015Article
- Structural insights into the functional versatility of WW domain-containing oxidoreductase tumor suppressor.Experimental biology and medicine (Maywood, N.J.) · 2015Review
- Regulation of cell signaling and apoptosis by tumor suppressor WWOX.Experimental biology and medicine (Maywood, N.J.) · 2015Review
- Versatile communication strategies among tandem WW domain repeats.Experimental biology and medicine (Maywood, N.J.) · 2015Review
- MicroRNA-153 promotes Wnt/β-catenin activation in hepatocellular carcinoma through suppression of WWOX.Oncotarget · 2015Article
- Ligand binding to WW tandem domains of YAP2 transcriptional regulator is under negative cooperativity.The FEBS journal · 2014Article
- WWOX at the crossroads of cancer, metabolic syndrome related traits and CNS pathologies.Biochimica et biophysica acta · 2014Review
- Characterizing WW domain interactions of tumor suppressor WWOX reveals its association with multiprotein networks.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The ability of WWOX tumor suppressor to physically associate with the intracellular domain (ICD) of ErbB4 receptor tyrosine kinase is believed to play a central role in downregulating the transcriptional function of the latter. Herein, using various biophysical methods, we show that while the WW1 domain of WWOX binds to PPXY motifs located within the ICD of ErbB4 in a physiologically relevant manner, the WW2 domain does not. Importantly, while the WW1 domain absolutely requires the integrity of the PPXY consensus sequence, nonconsensus residues within and flanking this motif do not appear to be critical for binding. This strongly suggests that the WW1 domain of WWOX is rather promiscuous toward its cellular partners. We also provide evidence that the lack of binding of the WW2 domain of WWOX to PPXY motifs is due to the replacement of a signature tryptophan, lining the hydrophobic ligand binding groove, with tyrosine (Y85). Consistent with this notion, the Y85W substitution within the WW2 domain exquisitely restores its binding to PPXY motifs in a manner akin to the binding of the WW1 domain of WWOX. Of particular significance is the observation that the WW2 domain augments the binding of the WW1 domain to ErbB4, implying that the former serves as a chaperone within the context of the WW1-WW2 tandem module of WWOX in agreement with our findings reported previously. Altogether, our study sheds new light on the molecular basis of an important WW-ligand interaction involved in mediating a plethora 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.