EZH2 T367 phosphorylation activates p38 signaling through lysine methylation to promote breast cancer progression
Maria E. González, Giuseppina Daniela Naimo, Talha Anwar, Alessandro Paolì, Shilpa R. Tekula, Suny Kim, Natasha Medhora, Shoshana A. Leflein, Jacob Itkin, Raymond C. Trievel, Kelley M. Kidwell, Yu‐Chih Chen, Loredana Mauro, Euisik Yoon, Sebastiano Andò, Celina G. Kleer
Abstract
and reduces TNBC growth and metastasis. These data uncover a cooperation between EZH2 canonical and non-canonical mechanisms and suggest that inhibition of these pathways may be a potential therapeutic strategy.
Topics & Concepts
EZH2Histone methyltransferaseCancer researchPhosphorylationHistone H3p38 mitogen-activated protein kinasesHistoneLysineMethyltransferaseMethylationAcetylationMetastasisPRC2BiologyChemistryCell biologyCancerBiochemistryProtein kinase AGeneticsAmino acidGeneEpigenetics and DNA MethylationGenomics and Chromatin DynamicsRNA modifications and cancer