|  Help  |  About  |  Contact Us

Publication : Serine 347 Phosphorylation by JNKs Negatively Regulates OCT4 Protein Stability in Mouse Embryonic Stem Cells.

First Author  Bae KB Year  2017
Journal  Stem Cell Reports Volume  9
Issue  6 Pages  2050-2064
PubMed ID  29153991 Mgi Jnum  J:259122
Mgi Id  MGI:6148490 Doi  10.1016/j.stemcr.2017.10.017
Citation  Bae KB, et al. (2017) Serine 347 Phosphorylation by JNKs Negatively Regulates OCT4 Protein Stability in Mouse Embryonic Stem Cells. Stem Cell Reports 9(6):2050-2064
abstractText  The POU transcription factor OCT4 is critical for maintaining the undifferentiated state of embryonic stem cells (ESCs) and generating induced pluripotent stem cells (iPSCs), but its precise mechanisms of action remain poorly understood. Here, we investigated the role of OCT4 phosphorylation in the biological functions of ESCs. We observed that c-Jun N-terminal kinases (JNKs) directly interacted with and phosphorylated OCT4 at serine 347, which inhibited the transcriptional activity of OCT4. Moreover, phosphorylation of OCT4 induced binding of FBXW8, which reduced OCT4 protein stability and enhanced its proteasomal degradation. We also found that the mutant OCT4 (S347A) might delay the differentiation process of mouse ESCs and enhance the efficiency of generating iPSCs. These results demonstrated that OCT4 phosphorylation on serine 347 by JNKs plays an important role in its stability, transcriptional activities, and self-renewal of mouse ESCs.
Quick Links:
 
Quick Links:
 

Expression

Publication --> Expression annotations

 

Other

13 Bio Entities

Trail: Publication

0 Expression