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A paREDOX in the control of cholesterol biosynthesis: Does the NADPH sensor and E3 ubiquitin ligase MARCHF6 protect mammalian cells during oxidative stress by controlling sterol biosynthesis?

Fenton, Nicole M., Qian, Lydia, Paine, Eloise G., Sharpe, Laura J., Brown, Andrew J.·2024·BioEssays
DOI 10.1002/bies.202400073
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Abstract

Sterols and the reductant nicotinamide adenine dinucleotide phosphate (NADPH), essential for eukaryotic life, arose because of, and as an adaptation to, rising levels of molecular oxygen (O 2). Hence, the NADPH and O 2‐intensive process of sterol biosynthesis is inextricably linked to redox status. In mammals, cholesterol biosynthesis is exquisitely regulated post‐translationally by multiple E3 ubiquitin ligases, with membrane associated Really Interesting New Gene (RING) C 3 HC 4 finger 6 (MARCHF6) degrading at least six enzymes in the pathway. Intriguingly, all these MARCHF6‐dependent enzymes require NADPH. Moreover, MARCHF6 is activated by NADPH, although what this means for control of cholesterol synthesis is unclear. Indeed, this presents a paradox for how NADPH regulates this vital pathway, since NADPH is a cofactor in cholesterol biosynthesis and yet, low levels of NADPH should spare cholesterol biosynthesis enzymes targeted by MARCHF6 by reducing its activity. We speculate MARCHF6 helps mammalian cells adapt to oxidative stress (signified by low NADPH levels) by reducing degradation of cholesterogenic enzymes, thereby maintaining synthesis of protective cholesterol.

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Metadata

Authors
Fenton, N. M., Qian, L., Paine, E. G., Sharpe, L. J., & Brown, A. J.
Affiliations
School of Biotechnology and Biomolecular Sciences University of New South Wales Sydney NSW Australia
ORCID
Brown, Andrew J.
Venue
BioEssays
Publisher
Wiley
Published
2024-05-17
Volume
46
Issue
7
ISSN
  • 0265-9247
  • 1521-1878
DOI
10.1002/bies.202400073
Cited by
7
References
2
Language
en
Licence
creativecommons.org/licenses/by-nc/4.0/ (vor)

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