{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Prof. Wenqi Wang"],"funding":["HHS | National Institutes of Health (NIH)","U.S. Department of Defense (DOD)","American Cancer Society (ACS)","HHS | NIH | National Cancer Institute (NCI)","HHS | NIH | National Institute of General Medical Sciences (NIGMS)"],"journal":["The EMBO Journal"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-SCDT-EMBOJ-2019-102406"],"abstract":["The Hippo pathway, which plays a critical role in organ size control and cancer, features numerous WW domain-based protein-protein interactions. However, ~100 WW domains and 2,000 PY motif-containing peptide ligands are found in the human proteome, raising a \"WW-PY\" binding specificity issue in the Hippo pathway. In this study, we have established the WW domain binding specificity for Hippo pathway components and uncovered a unique amino acid sequence required for it. By using this criterion, we have identified a WW domain-containing protein, STXBP4, as a negative regulator of YAP. Mechanistically, STXBP4 assembles a protein complex comprising ?-catenin and a group of Hippo PY motif-containing components/regulators to inhibit YAP, a process that is regulated by actin cytoskeleton tension. "],"repository":["biostudies-other"],"funding_grant_id":["W81XWH-09-1-0409","GM055246","P30 CA062203","RSG-18-009-01-CCG","GM130367","GM126048","T32 EB009418-08"],"pubmed_authors":["Vy, Thuy Duong","Prof. Junjie Chen","Kimberly Chuc","Sunwoo Oh","Albert, Paul Ta","Olga Razorenova","Yuxuan Chen","Prof. Ray Luo","Prof. Wenqi Wang","Xu Li","Han Han","Shiji Zhao","Ms. Bing Yang","Amal, El Ali","Rebecca Vargas","Gayoung Seo"],"additional_accession":[]},"is_claimable":false,"name":"Elucidation of WW domain ligand binding specificities in the Hippo pathway reveals STXBP4 as YAP inhibitor","description":"The Hippo pathway, which plays a critical role in organ size control and cancer, features numerous WW domain-based protein-protein interactions. However, ~100 WW domains and 2,000 PY motif-containing peptide ligands are found in the human proteome, raising a \"WW-PY\" binding specificity issue in the Hippo pathway. In this study, we have established the WW domain binding specificity for Hippo pathway components and uncovered a unique amino acid sequence required for it. By using this criterion, we have identified a WW domain-containing protein, STXBP4, as a negative regulator of YAP. Mechanistically, STXBP4 assembles a protein complex comprising ?-catenin and a group of Hippo PY motif-containing components/regulators to inhibit YAP, a process that is regulated by actin cytoskeleton tension. ","dates":{"release":"2020-01-13T21:00:54Z","modification":"2020-01-13T21:00:54Z","creation":"2020-01-13T21:00:54Z"},"accession":"S-SCDT-EMBOJ-2019-102406","cross_references":{"doi":["10.15252/embj.2019102406"]}}