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 article

4 Citations (Scopus)
89 Downloads (Pure)

Abstract

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
Volume429
Issue number10
Early online date26 Apr 2017
DOIs
Publication statusPublished - 19 May 2017

Fingerprint

Protein Kinases
Phosphorylation
Embryonic Stem Cells
MAP Kinase Signaling System
Fibroblast Growth Factor 2
Post Translational Protein Processing
Phosphatidylinositol 3-Kinases
Cell Cycle
Phosphotransferases
Maintenance

Keywords

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

Cite this

@article{19aec91531bd49c79d9de1f2c949d3dc,
title = "Protein Kinases in Pluripotency - Beyond the Usual Suspects",
abstract = "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.",
keywords = "Pluripotency, Phosphorylation, Kinase, Embryonic Stem Cells, Signalling networks",
author = "Rosalia Fernandez-Alonso and Francisco Bustos and Williams, {Charles A. C.} and Findlay, {Greg M.}",
note = "The authors would like to apologise to those whose work could not be cited due to space limitations. C.A.C.W. is the recipient of an MRC PhD studentship and G.M.F. is supported in part by a Medical Research Council New Investigator Award (MR/N000609/1) and a Tenovus Scotland research grant (T15/11)",
year = "2017",
month = "5",
day = "19",
doi = "10.1016/j.jmb.2017.04.013",
language = "English",
volume = "429",
pages = "1504--1520",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Elsevier",
number = "10",

}

Protein Kinases in Pluripotency - Beyond the Usual Suspects. / Fernandez-Alonso, Rosalia; Bustos, Francisco; Williams, Charles A. C.; Findlay, Greg M. (Lead / Corresponding author).

In: Journal of Molecular Biology, Vol. 429, No. 10, 19.05.2017, p. 1504-1520.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Protein Kinases in Pluripotency - Beyond the Usual Suspects

AU - Fernandez-Alonso, Rosalia

AU - Bustos, Francisco

AU - Williams, Charles A. C.

AU - Findlay, Greg M.

N1 - The authors would like to apologise to those whose work could not be cited due to space limitations. C.A.C.W. is the recipient of an MRC PhD studentship and G.M.F. is supported in part by a Medical Research Council New Investigator Award (MR/N000609/1) and a Tenovus Scotland research grant (T15/11)

PY - 2017/5/19

Y1 - 2017/5/19

N2 - 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.

AB - 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.

KW - Pluripotency

KW - Phosphorylation

KW - Kinase

KW - Embryonic Stem Cells

KW - Signalling networks

U2 - 10.1016/j.jmb.2017.04.013

DO - 10.1016/j.jmb.2017.04.013

M3 - Review article

C2 - 28456524

VL - 429

SP - 1504

EP - 1520

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 10

ER -