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The protein HMG20A is predicted by the AlphaFold2 software to contain three distinct structural elements, which we have functionally characterized: i) an amino-terminal, intrinsically disordered domain with transactivation activity; ii) an HMG box with higher binding affinity for double-stranded, four-way-junction DNA than for linear DNA; and iii) a long coiled-coil domain. Our proteomic study followed by a deletion analysis and structural modeling demonstrates that HMG20A forms a complex with the histone reader PHF14, via the establishment of a two-stranded alpha-helical coiled-coil structure. siRNA-mediated knockdown of either PHF14 or HMG20A in MDA-MB-231 cells causes similar defects in cell migration, invasion and homotypic cell\u2013cell adhesion ability, but neither affects proliferation. Transcriptomic analyses demonstrate that PHF14 and HMG20A share a large subset of targets. We show that the PHF14-HMG20A complex modulates the Hippo pathway through a direct interaction with the TEAD1 transcription factor. PHF14 or HMG20A deficiency increases epithelial markers, including E-cadherin and the epithelial master regulator TP63 and impaired normal TGF\u03b2-trigged epithelial-to-mesenchymal transition. Taken together, these data indicate that PHF14 and HMG20A cooperate in regulating several pathways involved in epithelial\u2013mesenchymal plasticity.<\/jats:p>","DOI":"10.1093\/nar\/gkac766","type":"journal-article","created":{"date-parts":[[2022,9,15]],"date-time":"2022-09-15T09:59:28Z","timestamp":1663235968000},"page":"9838-9857","source":"Crossref","is-referenced-by-count":9,"title":["The high mobility group protein HMG20A cooperates with the histone reader PHF14 to modulate TGF\u03b2 and Hippo pathways"],"prefix":"10.1093","volume":"50","author":[{"given":"Elena","family":"G\u00f3mez-Mar\u00edn","sequence":"first","affiliation":[{"name":"Genome Biology Department. Centro Andaluz de Biolog\u00eda Molecular y Medicina Regenerativa-CABIMER, Consejo Superior de Investigaciones Cient\u00edficas-Universidad de Sevilla-Universidad Pablo de Olavide (CSIC-USE-UPO) , Av. 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Centro Andaluz de Biolog\u00eda Molecular y Medicina Regenerativa-CABIMER, Consejo Superior de Investigaciones Cient\u00edficas-Universidad de Sevilla-Universidad Pablo de Olavide (CSIC-USE-UPO) , Av. Americo Vespucio, 41092 Seville , Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9\u00a0A","family":"Guerrero-Mart\u00ednez","sequence":"additional","affiliation":[{"name":"Genome Biology Department. Centro Andaluz de Biolog\u00eda Molecular y Medicina Regenerativa-CABIMER, Consejo Superior de Investigaciones Cient\u00edficas-Universidad de Sevilla-Universidad Pablo de Olavide (CSIC-USE-UPO) , Av. Americo Vespucio, 41092 Seville , Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gonzalo","family":"Arribas","sequence":"additional","affiliation":[{"name":"Genome Biology Department. 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Centro Andaluz de Biolog\u00eda Molecular y Medicina Regenerativa-CABIMER, Consejo Superior de Investigaciones Cient\u00edficas-Universidad de Sevilla-Universidad Pablo de Olavide (CSIC-USE-UPO) , Av. Americo Vespucio, 41092 Seville , Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuel","family":"Rodr\u00edguez-Paredes","sequence":"additional","affiliation":[{"name":"Institute of Toxicology, University Medical Center Mainz, Johannes Gutenberg University , 55131 Mainz , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mercedes","family":"Tom\u00e9","sequence":"additional","affiliation":[{"name":"Cell Dynamics and Signaling Department. Centro Andaluz de Biolog\u00eda Molecular y Medicina Regenerativa-CABIMER, Consejo Superior de Investigaciones Cient\u00edficas-Universidad de Sevilla-Universidad Pablo de Olavide (CSIC-USE-UPO) , Av. 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