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Post-translational modification of proteins by phosphorylation plays a key role in regulating all aspects of eukaryotic biology. Embryonic Stem Cell (ESC) pluripotency, defined as the ability to differentiate into all cell types in the adult body, is no exception. Maintenance and dissolution of pluripotency is tightly controlled by phosphorylation. As a result, key signalling pathways that regulate pluripotency have been identified and their functions well characterised. Amongst the best studied are the FGF-ERK1/2 pathway, PI3K-AKT, the LIF-JAK-STAT3 axis, WNT-GSK3 signalling and the TGFβ/BMP family. However, these kinase pathways constitute only a small proportion of the protein kinase complement of pluripotent cells, and there is accumulating evidence that diverse phosphorylation systems modulate ESC pluripotency. Here, we review recent progress in understanding the overarching role of phosphorylation in mediating communication from the cellular environment, metabolism and cell cycle to the core pluripotency machinery.
|Number of pages||17|
|Journal||Journal of Molecular Biology|
|Early online date||26 Apr 2017|
|Publication status||Published - 19 May 2017|
- Embryonic Stem Cells
- Signalling networks
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- 1 Finished
Elucidating Novel Pluripotency Signalling Networks (New Investigator Award)
1/09/15 → 31/08/18
Identification of the ERK5 Kinase as a Key Regulator of Embryonic Stem Cell PluripotencyAuthor: Williams, C., 2017
Supervisor: Findlay, G. (Supervisor)
Student thesis: Doctoral Thesis › Doctor of Philosophy