Protein Kinases in Pluripotency - Beyond the Usual Suspects

Rosalia Fernandez-Alonso, Francisco Bustos, Charles A. C. Williams, Greg M. Findlay (Lead / Corresponding author)

Research output: Contribution to journalReview articlepeer-review

16 Citations (Scopus)
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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.
Original languageEnglish
Pages (from-to)1504-1520
Number of pages17
JournalJournal of Molecular Biology
Issue number10
Early online date26 Apr 2017
Publication statusPublished - 19 May 2017


  • Pluripotency
  • Phosphorylation
  • Kinase
  • Embryonic Stem Cells
  • Signalling networks


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