University of Oulu

Albanese, A.; Daly, L.A.; Mennerich, D.; Kietzmann, T.; Sée, V. The Role of Hypoxia-Inducible Factor Post-Translational Modifications in Regulating Its Localisation, Stability, and Activity. Int. J. Mol. Sci. 2021, 22, 268.

The role of hypoxia-inducible factor post-translational modifications in regulating its localisation, stability, and activity

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Author: Albanese, Adam1; Daly, Leonard A.2; Mennerich, Daniela3;
Organizations: 1Department of Molecular Physiology and Cell Signalling, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L697ZB, UK
2Department of Biochemistry and System Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L697ZB, UK
3Faculty of Biochemistry and Molecular Medicine, Biocenter Oulu, University of Oulu, FI-90014 Oulu, Finland
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 3.7 MB)
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Language: English
Published: Multidisciplinary Digital Publishing Institute, 2021
Publish Date: 2021-03-29


The hypoxia signalling pathway enables adaptation of cells to decreased oxygen availability. When oxygen becomes limiting, the central transcription factors of the pathway, hypoxia-inducible factors (HIFs), are stabilised and activated to induce the expression of hypoxia-regulated genes, thereby maintaining cellular homeostasis. Whilst hydroxylation has been thoroughly described as the major and canonical modification of the HIF-α subunits, regulating both HIF stability and activity, a range of other post-translational modifications decorating the entire protein play also a crucial role in altering HIF localisation, stability, and activity. These modifications, their conservation throughout evolution, and their effects on HIF-dependent signalling are discussed in this review.

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Series: International journal of molecular sciences
ISSN: 1661-6596
ISSN-E: 1422-0067
ISSN-L: 1661-6596
Volume: 22
Issue: 1
Article number: 268
DOI: 10.3390/ijms22010268
Type of Publication: A2 Review article in a scientific journal
Field of Science: 1182 Biochemistry, cell and molecular biology
116 Chemical sciences
Funding: A.A. is a recipient of a MRC DiMeN studentship. L.A.D. is supported by BBSRC. T.K. is supported by the Academy of Finland SA296027, the Jane and Aatos Erkko Foundation, the Finnish Cancer Foundation, the Sigrid Juselius Foundation, the University of Oulu, and Biocenter Oulu. All authors have read and agreed to the published version of the manuscript.
Academy of Finland Grant Number: 296027
Detailed Information: 296027 (Academy of Finland Funding decision)
Copyright information: © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (