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2-Oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2

Lookup NU author(s): Dr Tom McAllisterORCiD, Professor Akane KawamuraORCiD

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

© 2018 The Royal Society of Chemistry. Prolyl hydroxylation of hypoxia inducible factor (HIF)-α, as catalysed by the Fe(ii)/2-oxoglutarate (2OG)-dependent prolyl hydroxylase domain (PHD) enzymes, has a hypoxia sensing role in animals. We report that binding of prolyl-hydroxylated HIF-α to PHD2 is ∼50 fold hindered by prior 2OG binding; thus, when 2OG is limiting, HIF-α degradation might be inhibited by PHD binding.

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Author(s): Abboud MI, McAllister TE, Leung IKH, Chowdhury R, Jorgensen C, Domene C, Mecinovic J, Lippl K, Hancock RL, Hopkinson RJ, Kawamura A, Claridge TDW, Schofield CJ

Publication type: Article

Publication status: Published

Journal: Chemical Communications

Year: 2018

Volume: 54

Issue: 25

Pages: 3130-3133

Print publication date: 28/03/2018

Online publication date: 09/03/2018

Acceptance date: 31/01/2018

Date deposited: 14/10/2019

ISSN (print): 1359-7345

ISSN (electronic): 1364-548X

Publisher: Royal Society of Chemistry

URL: https://doi.org/10.1039/c8cc00387d

DOI: 10.1039/c8cc00387d

PubMed id: 29522057

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