NADH binds and stabilizes the 26S proteasomes independent of ATP
Open accessAbstract
The 26S proteasome is the end point of the ubiquitin- and ATP-dependent degradation pathway. The 26S proteasome complex (26S PC) integrity and function has been shown to be highly dependent on ATP and its homolog nucleotides. We report here that the redox molecule NADH binds the 26S PC and is sufficient in maintaining 26S PC integrity even in the absence of ATP. Five of the 19S proteasome complex subunits contain a putative NADH binding motif (G x G xx G) including the AAA-ATPase subunit, Psmc1 (Rpt2). We demonstrate that recombinant Psmc1 binds NADH via the G x G xx G motif. Introducing the ΔG x G xx G Psmc1 mutant into cells results in reduced NADH-stabilized 26S proteasomes and decreased viability following redox stress induced by the mitochondrial inhibitor rotenone. The newly identified NADH binding of 26S proteasomes advances our understanding of the molecular mechanisms of protein degradation and highlights a new link between protein homeostasis and the cellular metabolic/redox state. Background: 26S proteasome complex is highly dependent on ATP. Results: NADH binds the proteasome via the Psmc1 subunit resulting in ATP-independent stabilization of the 26S proteasome complex, in vitro and in cells. Conclusion: NADH is a novel regulator of the 26S proteasome. Significance: NADH can maintain proteasomal integrity in the absence of ATP, linking cellular redox state to protein degradation.
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NADH binds and stabilizes 26S proteasomes and may also regulate 20S proteasomes.
“Interestingly, the reduced form of NAD+, NADH, binds and stabilizes 26S proteasomes, and may also regulate the function of 20S proteasomes, the two main proteolytic complexes (Asher et al., 2005; Tsvetkov et al., 2014).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Tsvetkov et al., 2014
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- Authors
- Tsvetkov, P., Myers, N., Eliav, R., Adamovich, Y., Hagai, T., Adler, J., Navon, A., & Shaul, Y.
- Affiliations
- University of California, San Francisco (US)
- Weizmann Institute of Science (IL)
- Corresponding author
- Tsvetkov, Peter
- Shaul, Yosef
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 289
- Issue
- 16
- Pages
- 11272-11281
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC4036265
- OpenAlex
- W2008467857
- Cited by
- 42
- References
- 42
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 4 · 2022: 4 · 2021: 2 · 2020: 4 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 2 · 2015: 3 · 2014: 3
- FWCI
- 1.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- 26S proteasome, NADH binding, Rpt2, AAA+ ATPase, redox stress, rotenone, protein degradation, ubiquitin-proteasome system, proteostasis, redox state
- MeSH terms
- Animals, Enzyme Stability, Humans, Male, Mice, Inbred ICR, NADP, Oxidation-Reduction, Protein Binding, Amino Acid Motifs, NIH 3T3 Cells, Proteasome Endopeptidase Complex, Mice, HEK293 Cells, Proteolysis
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