Role of Hepatocyte-like Cells in the Differentiation of Cardiomyocytes from Mouse Embryonic Stem Cells

2005 ◽  
Vol 14 (2) ◽  
pp. 153-161 ◽  
Author(s):  
Rajarshi Pal ◽  
Aparna Khanna
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cells

scholarly journals The role of BMP signaling in mouse embryonic stem cells

2011 ◽  
Vol 356 (1) ◽  
pp. 213
Author(s):  
Mui Nhuc Luong ◽  
Ira Blitz ◽  
Jin Cho ◽  
Kenny Daily ◽  
Vishal Patel ◽  
...  
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cells ◽  
Bmp Signaling

scholarly journals A new puzzling role of p53 in mouse embryonic stem cells

Cell Cycle ◽  
2010 ◽  
Vol 9 (9) ◽  
pp. 1669-1670 ◽  
Author(s):  
Mangmang Li ◽  
Jing Huang
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Embryonic Stem ◽  
Mouse Embryonic Stem Cells

scholarly journals Arginine methylation of METTL14 promotes RNA N6-methyladenosine modification and endoderm differentiation of mouse embryonic stem cells

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Xiaona Liu ◽  
Hailong Wang ◽  
Xueya Zhao ◽  
Qizhi Luo ◽  
Qingwen Wang ◽  
...  
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Mutant Mouse ◽  
Embryonic Stem ◽  
Arginine Methylation ◽  
Mouse Embryonic Stem Cells ◽  
Protein Methylation ◽  
Dynamic Regulation ◽  
Endoderm Differentiation

AbstractRNA N6-methyladenosine (m6A), the most abundant internal modification of mRNAs, plays key roles in human development and health. Post-translational methylation of proteins is often critical for the dynamic regulation of enzymatic activity. However, the role of methylation of the core methyltransferase METTL3/METTL14 in m6A regulation remains elusive. We find by mass spectrometry that METTL14 arginine 255 (R255) is methylated (R255me). Global mRNA m6A levels are greatly decreased in METTL14 R255K mutant mouse embryonic stem cells (mESCs). We further find that R255me greatly enhances the interaction of METTL3/METTL14 with WTAP and promotes the binding of the complex to substrate RNA. We show that protein arginine N-methyltransferases 1 (PRMT1) interacts with and methylates METTL14 at R255, and consistent with this, loss of PRMT1 reduces mRNA m6A modification globally. Lastly, we find that loss of R255me preferentially affects endoderm differentiation in mESCs. Collectively, our findings show that arginine methylation of METTL14 stabilizes the binding of the m6A methyltransferase complex to its substrate RNA, thereby promoting global m6A modification and mESC endoderm differentiation. This work highlights the crosstalk between protein methylation and RNA methylation in gene expression.

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