2026-04-29T22:57:47Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/260832025-12-18T12:57:07Zcom_20.500.12105_2327com_20.500.12105_2290col_20.500.12105_16991
Repisalud
author
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
funder
European Union (EU)
funder
Ikerbasque
funder
Spanish Association Against Cancer (AECC)
funder
Comunidad de Madrid
2025-01-21T11:16:40Z
2025-01-21T11:16:40Z
2023-05-25
Nat Commun . 2023 May 25;14(1):3016.
Nature Communications
37230995
https://hdl.handle.net/20.500.12105/26083
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.
eng
EMBRYONIC STEM-CELLS
DNA METHYLATION
REVEALS
EZH2
PRMT5
METHYLTRANSFERASES
CHROMATINMARKS
Decoding protein methylation function with thermal stability analysis.
research article
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