2026-04-29T22:57:45Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/260832025-12-18T12:57:07Zcom_20.500.12105_2327com_20.500.12105_2290col_20.500.12105_16991

00925njm 22002777a 4500 dc Sayago, Cristina author Sánchez-Wandelmer, Jana author García, Fernando author Hurtado, Begoña author Lafarga, Vanesa author Prieto, Patricia author Zarzuela, Eduardo author Ximénez-Embún, Pilar author Ortega Jimenez, Sagrario author Megías, Diego author Fernandez-Capetillo, Oscar author Malumbres, Marcos author Munoz, Javier author 2023-05-25 Protein methylation is an important modification beyond epigenetics. However, systems analyses of protein methylation lag behind compared to other modifications. Recently, thermal stability analyses have been developed which provide a proxy of a protein functional status. Here, we show that molecular and functional events closely linked to protein methylation can be revealed by the analysis of thermal stability. Using mouse embryonic stem cells as a model, we show that Prmt5 regulates mRNA binding proteins that are enriched in intrinsically disordered regions and involved in liquid-liquid phase separation mechanisms, including the formation of stress granules. Moreover, we reveal a non-canonical function of Ezh2 in mitotic chromosomes and the perichromosomal layer, and identify Mki67 as a putative Ezh2 substrate. Our approach provides an opportunity to systematically explore protein methylation function and represents a rich resource for understanding its role in pluripotency. Nat Commun . 2023 May 25;14(1):3016. Nature Communications 37230995 https://hdl.handle.net/20.500.12105/26083 EMBRYONIC STEM-CELLS DNA METHYLATION REVEALS EZH2 PRMT5 METHYLTRANSFERASES CHROMATINMARKS Decoding protein methylation function with thermal stability analysis.