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Cell death

Hypoxia-stabilized RIPK1 promotes cell death

Nature Cell Biology volume 25, pages 921–922 (2023)Cite this article

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The PHD–pVHL pathway is essential for oxygen-dependent prolyl hydroxylation of HIFA. A recent study identifies RIPK1 as a hydroxylation target in this pathway during hypoxia-induced cell death and presents a 2.8 Å resolution crystal structure of the pVHL–elongin B/C complex bound to hydroxylated RIPK1.

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Fig. 1: Divergent pathways and functions of RIPK1 and HIFA under hypoxia.

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Authors and Affiliations

  1. Department of Anesthesiology, Critical Care and Pain Medicine, McGovern Medical School, The University of Texas Health Science Center at Houston, Houston, TX, USA

    Wei Ruan, Holger K. Eltzschig & Xiaoyi Yuan

  2. Outcomes Research Consortium, Cleveland, OH, USA

    Holger K. Eltzschig

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  1. Wei Ruan
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  2. Holger K. Eltzschig
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  3. Xiaoyi Yuan
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Correspondence to Xiaoyi Yuan.

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Competing interests

W.R. receives research funding from IARS Mentored Research Award. H.K.E. receives research funding from National Institute of Health (NIH) grants R01HL154720, R01DK122796, R01DK109574, R01HL133900 and Department of Defense grant W81XWH2110032. X.Y. receives research funding from NIH grant R01HL155950, and a Parker B. Francis fellowship. H.K.E. and X.Y. received research funding through a contract between Akebia Therapeutics and UTHealth to support a clinical trial on the effect of vadadustat in hospitalized patients with COVID-19 (ClinicalTrials.gov identifier NCT04478071).

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Ruan, W., Eltzschig, H.K. & Yuan, X. Hypoxia-stabilized RIPK1 promotes cell death. Nat Cell Biol 25, 921–922 (2023). https://doi.org/10.1038/s41556-023-01176-y

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