UCP2, not a physiologically relevant uncoupler but a glucose sparing switch impacting ROS production and glucose sensing
Open accessAbstract
In mammals the two proteins UCP2 and UCP3 are highly similar to the mitochondrial uncoupling protein found in the brown adipose tissue (UCP1). Accordingly, it was proposed that UCP2 and UCP3 are also uncoupling proteins i.e. protonophores with impact on mitochondrial ROS production and glucose signaling. However, it appears now impossible to explain the physiological relevance of the new UCPs uniquely by their uncoupling activity as observed in vitro. Therefore, we propose a metabolic hypothesis in which UCP2 acts through a transport distinct of the proton transport. A consequence of this transport activity would be a decrease of the mitochondrial oxidation of the pyruvate originating from glucose. This would put UCP2 and UCP3 in a crucial position to influence cellular metabolism. The tight control exerted on UCP2 expression appears consistent with it. In this hypothesis, UCP2/3 would allow a cell to remain glycolytic within an aerobic organism. This tallies with the high expression level of UCP2 or UCP3 in glycolytic cells. The metabolic hypothesis would explain the spectacular modifications associated with UCP2 manipulation as well as the uncoupling activity usually called for and which in fact remains elusive in vivo.
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Strong evidence of mitochondrial uncoupling property is clear for UCP-1 but still heavily debated for other UCPs.
“Importantly, although strong evidence of the mitochondrial uncoupling property is clear for UCP-1 [7,12], it is still heavily debated for the other UCPs [13,14,15].”
From Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases (2019) · cites this paper as [13]
The critical role of UCP2 in promoting aerobic glycolysis and inhibiting oxidative phosphorylation has been established from multiple experimental models.
“the critical role of UCP2 (uncoupling protein 2) in promoting aerobic glycolysis and inhibiting oxidative phosphorylation has been established from multiple experimental models (Pecqueur et al., 2008; Samudio et al., 2008; Bouillaud, 2009; Zhang et al., 2011).”
From Metabolic reprogramming during neuronal differentiation from aerobic glycolysis to neuronal oxidative phosphorylation (2016) · cites this paper as Bouillaud, 2009
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- Authors
- Bouillaud, F.
- Affiliations
- Hôpital Necker-Enfants Malades (FR)
- Corresponding author
- Bouillaud, Frédéric
- ORCID
- Bouillaud, Frédéric
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 1787
- Issue
- 5
- Pages
- 377-383
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2018720754
- Cited by
- 146
- References
- 57
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 5 · 2023: 12 · 2022: 6 · 2021: 10 · 2020: 7 · 2019: 7 · 2018: 8 · 2017: 11 · 2016: 11 · 2015: 10 · 2014: 5 · 2013: 11 · 2012: 5
- FWCI
- 0.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission (ECFP6, LSHM‐CT‐2003‐503041)
- Agence Nationale de la Recherche
- Institut National de la Santé et de la Recherche Médicale
- Centre National de la Recherche Scientifique
- Servier
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- UCP2, UCP3, mitochondrial uncoupling proteins, glucose sparing, mitochondrial reactive oxygen species, glucose detection, pyruvate oxidation, glycolysis, protonophores, mitochondrial metabolism
- MeSH terms
- Uncoupling Protein 2, Uncoupling Protein 3, Uncoupling Protein 1, Adenosine Triphosphate, Adipose Tissue, Aerobiosis, Animals, Adipose Tissue, Brown, Glucose, Glycolysis, Humans, Ion Channels, Mammals, Oxygen Consumption, Yeasts, Reactive Oxygen Species, Mitochondrial Proteins
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