Biosensor reveals multiple sources for mitochondrial NAD +
Open accessAbstract
A fluorescent sensor for NAD + in living cells: Roles of cellular nicotinamide adenine dinucleotide (NAD + ) in metabolism, aging, and disease have garnered much interest, but methods have been lacking to measure the amounts of NAD + in living cells. Cambronne et al. developed a genetically encoded biosensor that can be used to monitor concentrations of free NAD + in various compartments of a cell (see the Perspective by Guarente). Such concentrations of NAD + appear to be important in regulating the activity of NAD + -consuming enzymes such as sirtuins and ADP-ribosyltransferases. The authors used the sensor to demonstrate that NAD + concentrations in mitochondria of cultured human cells can be controlled by multiple mechanisms. Science , this issue p. 1474 ; see also p. 1396
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The enzymes involved in NAD+ biosynthesis or degradation are highly compartmentalized.
“These pools are regulated independently of each other, and consistent with this, the enzymes involved in the biosynthesis or degradation of NAD+ are highly compartmentalized as well2–4.”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [4]
NAD+ is highly compartmentalized in the cytoplasm, mitochondria and nucleus, which are its main subcellular pools.
“NAD+ is highly compartmentalized in the cytoplasm, mitochondria and nucleus, which represent its main subcellular pools (Supplementary Box 1).”
From NAD+ metabolism and its roles in cellular processes during ageing (2021) · cites this paper as [4]
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References 20 · Cited by 407
- Authors
- Cambronne, X. A., Stewart, M. L., Kim, D., Jones-Brunette, A. M., Morgan, R. K., Farrens, D. L., Cohen, M. S., & Goodman, R. H.
- Affiliations
- Oregon Health & Science University (US)
- Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, OR 97239, USA.
- Corresponding author
- Cambronne, Xiaolu A.
- Cohen, Michael S.
- Venue
- Science
- Published
- 2016-06-17
- Volume
- 352
- Issue
- 6292
- Pages
- 1474-1477
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC6530784
- OpenAlex
- W2432789362
- Cited by
- 407
- References
- 20
- Citations by year
- 2026: 45 · 2025: 40 · 2024: 35 · 2023: 30 · 2022: 51 · 2021: 47 · 2020: 46 · 2019: 29 · 2018: 38 · 2017: 33 · 2016: 13
- FWCI
- 21.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Pew Charitable Trust
- NIH (NS088629, UL1TR000128, P30NS061800, P30CA069533)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- NAD+, genetically encoded fluorescent sensors, sirtuins, poly(ADP-ribose) polymerase, subcellular compartmentalization, NAD biosynthesis, Michaelis constant, NAD+ depletion
- MeSH terms
- Bacterial Proteins, Binding Sites, Cell Nucleus, Cytoplasm, Cytosol, HeLa Cells, Humans, Luminescent Proteins, Mitochondria, NAD, Nicotinamide-Nucleotide Adenylyltransferase, Poly(ADP-ribose) Polymerases, DNA Ligases, Biosensing Techniques, Point Mutation, Sirtuins, HEK293 Cells
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