Back to Search
Start Over
Cross-talk between Arg methylation and Ser phosphorylation modulates apoptosis signal–regulating kinase 1 activation in endothelial cells
- Source :
- Molecular Biology of the Cell
- Publication Year :
- 2016
- Publisher :
- American Society for Cell Biology (ASCB), 2016.
-
Abstract
- Protein arginine methyltransferase 5 interacts with and methylates apoptosis signal–regulating kinase 1 at arginine residue 89, thereby negatively regulating its activity by promoting the interaction between ASK1 and Akt and thus phosphorylating ASK1 at serine residue 83.<br />We describe a novel functional interaction between ASK1 and PRMT5. We show that PRMT5 interacts with and methylates ASK1 at arginine residue 89 and thereby negatively regulates its activity by promoting the interaction between ASK1 and Akt and thus phosphorylating ASK1 at serine residue 83. Furthermore, the association between ASK1 and Akt is enhanced by VEGF stimulation, and PRMT5 is required for this association. Moreover, PRMT5-mediated ASK1 methylation impaired the H2O2-induced activity of ASK1, and this inhibitory effect of PRMT5 was abolished by replacement of arginine 89 with Trp or depletion of PRMT5 expression by RNA interference. Together the results demonstrate cross-talk between arginine methylation and serine phosphorylation in ASK1.
- Subjects :
- Vascular Endothelial Growth Factor A
0301 basic medicine
Protein-Arginine N-Methyltransferases
Arginine
Biology
MAP Kinase Kinase Kinase 5
Methylation
Cell Line
Serine
03 medical and health sciences
0302 clinical medicine
Protein Interaction Mapping
Humans
Phosphorylation
Molecular Biology
Protein kinase B
Protein arginine methyltransferase 5
Endothelial Cells
Articles
Hydrogen Peroxide
Cell Biology
Molecular biology
Signaling
Enzyme Activation
030104 developmental biology
030220 oncology & carcinogenesis
Signal transduction
Proto-Oncogene Proteins c-akt
Signal Transduction
Subjects
Details
- ISSN :
- 19394586 and 10591524
- Volume :
- 27
- Database :
- OpenAIRE
- Journal :
- Molecular Biology of the Cell
- Accession number :
- edsair.doi.dedup.....13ddd64fd94ebff1bfe0743cd9365f93