The transcription factor Twist plays vital roles during embryonic development through regulating/controlling cell migration. However, postnatally, in normal physiological settings, Twist is either not expressed or inactivated. Increasing evidence shows a strong correlation between Twist reactivation and both cancer progression and malignancy, where the transcriptional activities of Twist support cancer cells to disseminate from primary tumours and subsequently establish a secondary tumour growth in distant organs. However, it is largely unclear how this signalling programme is reactivated or what signalling pathways regulate its activity. The present review discusses recent advances in Twist regulation and activity, with a focus on phosphorylation-dependent Twist activity, potential upstream kinases and the contribution of these factors in transducing biological signals from upstream signalling complexes. The recent advances in these areas have shed new light on how phosphorylation-dependent regulation of the Twist proteins promotes or suppresses Twist activity, leading to differential regulation of Twist transcriptional targets and thereby influencing cell fate.
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February 2012
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Conference Article|
January 19 2012
Phosphorylation of basic helix–loop–helix transcription factor Twist in development and disease
Gongda Xue;
Gongda Xue
1Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland
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Brian A. Hemmings
Brian A. Hemmings
1
1Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland
1To whom correspondence should be addressed (email Brian.Hemmings@fmi.ch).
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Publisher: Portland Press Ltd
Received:
July 28 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem Soc Trans (2012) 40 (1): 90–93.
Article history
Received:
July 28 2011
Citation
Gongda Xue, Brian A. Hemmings; Phosphorylation of basic helix–loop–helix transcription factor Twist in development and disease. Biochem Soc Trans 1 February 2012; 40 (1): 90–93. doi: https://doi.org/10.1042/BST20110678
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