.png){kind=icon}
.png){kind=icon}
Return
Decoding protein methylation function with thermal stability analysis
.png){kind=icon}
OA
AI
DOI：10.1038/s41467-023-38863-1.png)
.png){kind=icon}
.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
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. Methylation is a common modification that affects protein function but, compared to other modifications, our knowledge is limited. Here, the authors use a method based on thermal stability to study how protein methylation regulates processes such as mRNA binding proteins and chromosome compaction.
Keywords:
EMBRYONIC STEM-CELLS
DNA METHYLATION
REVEALS
EZH2
PRMT5
METHYLTRANSFERASES
CHROMATIN
MARKS
AI Summary
Key information extracted from the uploaded paper, including a brief overview, abstract, background, key highlights, visual analysis, and future outlook.
Journal
IF:
15.7
Papers:
9.2W
Citations:
91.2W