Research ResourceBiochemistry

Oxygen-dependent changes in binding partners and post-translational modifications regulate the abundance and activity of HIF-1α/2α

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Science Signaling  20 Jul 2021:
Vol. 14, Issue 692, eabf6685
DOI: 10.1126/scisignal.abf6685

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Stimulating and suppressing HIFs

Cells respond and adapt to hypoxia (low oxygen) in part by activating the α subunits of the HIF family of transcription factors. Daly et al. performed proteomics analysis of transfected cells to explore the protein modifications and binding partners for full-length versions of the hypoxia-response subunits HIF-1α and HIF-2α. Their findings, which included a phosphorylated cysteine, protein stability effects, and interactions with mitochondrial proteins, indicate that the oxygen-dependent regulation of HIF activity is more extensive and complex than was previously appreciated. This dataset will help to delineate the selective regulation and signaling mechanisms of these closely related isoforms in fine-tuning the cellular response to hypoxia.

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