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METTL3/METTL14 maintain human nucleoli integrity by mediating SUV39H1/H2 degradation
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METTL3/METTL14 maintain human nucleoli integrity by mediating SUV39H1/H2 degradation
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Journal Article
METTL3/METTL14 maintain human nucleoli integrity by mediating SUV39H1/H2 degradation
2024
Overview
Nucleoli are fundamentally essential sites for ribosome biogenesis in cells and formed by liquid-liquid phase separation (LLPS) for a multilayer condensate structure. How the nucleoli integrity is maintained remains poorly understood. Here, we reveal that METTL3/METTL14, the typical methyltransferase complex catalyzing N6-methyladnosine (m
6
A) on mRNAs maintain nucleoli integrity in human embryonic stem cells (hESCs). METTL3/METTL14 deficiency impairs nucleoli and leads to the complete loss of self-renewal in hESCs. We further show that SUV39H1/H2 protein, the methyltransferases catalyzing H3K9me3 were dramatically elevated in METTL3/METTL14 deficient cells, which causes an accumulation and infiltration of H3K9me3 across the whole nucleolus and impairs the LLPS. Mechanistically, METTL3/METTL14 complex serves as an essential adapter for CRL4 E3 ubiquitin ligase targeting SUV39H1/H2 for polyubiquitination and proteasomal degradation and therefore prevents H3K9me3 accumulation in nucleoli. Together, these findings uncover a previously unknown role of METTL3/METTL14 to maintain nucleoli integrity by facilitating SUV39H1/H2 degradation in human cells.
Nucleoli are essential cellular sites for ribosome biogenesis that are formed by liquid-liquid phase separation. Here the authors show that METTL3/METTL14 maintain nucleoli integrity through mediating SUV39H1/2 degradation in human embryonic stem cells.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/31
/ 13/51
/ 14/19
/ 14/28
/ 14/33
/ 38/91
/ 42/41
/ Histone-Lysine N-Methyltransferase
/ Human Embryonic Stem Cells - metabolism
/ Humanities and Social Sciences
/ Humans
/ Methyltransferases - genetics
/ Methyltransferases - metabolism
/ Nucleoli
/ Repressor Proteins - genetics
/ Repressor Proteins - metabolism
/ RNA
/ Science
/ Ubiquitin-Protein Ligases - genetics
/ Ubiquitin-Protein Ligases - metabolism
/ Yeast
