Oxygen-regulated post-translation modifications as master signalling pathway in cells.

Batie, Michael ORCID: 0000-0002-7508-6641, Fasanya, Temitope ORCID: 0009-0007-2107-8578, Kenneth, Niall S ORCID: 0000-0001-8528-1021 and Rocha, Sonia (2023) Oxygen-regulated post-translation modifications as master signalling pathway in cells. EMBO reports, 24 (12). e57849-e57849.

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Official URL: http://dx.doi.org/10.15252/embr.202357849

Abstract

Oxygen is essential for viability in mammalian organisms. However, cells are often exposed to changes in oxygen availability, due to either increased demand or reduced oxygen supply, herein called hypoxia. To be able to survive and/or adapt to hypoxia, cells activate a variety of signalling cascades resulting in changes to chromatin, gene expression, metabolism and viability. Cellular signalling is often mediated via post-translational modifications (PTMs), and this is no different in response to hypoxia. Many enzymes require oxygen for their activity and oxygen can directly influence several PTMS. Here, we review the direct impact of changes in oxygen availability on PTMs such as proline, asparagine, histidine and lysine hydroxylation, lysine and arginine methylation and cysteine dioxygenation, with a focus on mammalian systems. In addition, indirect hypoxia-dependent effects on phosphorylation, ubiquitination and sumoylation will also be discussed. Direct and indirect oxygen-regulated changes to PTMs are coordinated to achieve the cell's ultimate response to hypoxia. However, specific oxygen sensitivity and the functional relevance of some of the identified PTMs still require significant research.

Item Type:	Article
Uncontrolled Keywords:	Chromatin, Animals, Mammals, Humans, Oxygen, Lysine, Protein Processing, Post-Translational, Hypoxia
Divisions:	Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User:	Symplectic Admin
Date Deposited:	27 Oct 2023 09:41
Last Modified:	05 Jan 2024 09:21
DOI:	10.15252/embr.202357849
Open Access URL:	https://www.embopress.org/doi/full/10.15252/embr.2...
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3176480