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PLANT UNCOUPLING MITOCHONDRIAL PROTEIN 2 localizes to the Golgi
Open accessPreprint — published as 10.1093/plphys/kiad540
Abstract
Mitochondria act as cellular hubs of energy transformation and metabolite conversion in most eukaryotes. Plant mitochondrial electron transport chains are particularly flexible, featuring alternative components, such as ALTERNATIVE NAD(P)H DEHYDROGENASES and ALTERNATIVE OXIDASES (AOXs), that can bypass proton translocation steps. PLANT UNCOUPLING MITOCHONDRIAL PROTEINS (named PUMPs or plant UCPs) have been identified in plants as homologues of mammalian Uncoupling Proteins (UCPs), and their biochemical and physiological roles have been investigated in the context of mitochondrial energy metabolism. To dissect UCP function in Arabidopsis, the two most conserved (UCP1 and UCP2) have been targeted in recent work by combining mutant lines to circumvent potential functional redundancy in vivo . Such approaches rely on the assumption that both proteins reside in the inner mitochondrial membrane as a prerequisite for functional redundancy. Yet, contradicting results have been reported on UCP2 localization in plants. Here we provide evidence that, conversely to UCP1, which is an abundant inner mitochondrial membrane protein, UCP2 localizes to the Golgi rather than to mitochondria. Based on multiple lines of new and prior evidence, we summarize the consensus view that we have reached and provide an example of how open, critical exchange within the research community is able to constructively address ambiguities. Our observations and considerations provide direction to the ongoing discussion about the functions of UCP proteins. They further offer new perspectives for the study of Golgi membrane transport and subcellular targeting principles of membrane proteins. Since 20 to 30 % of genes in plant genomes are predicted to encode transmembrane proteins and the function of most of those proteins has not been experimentally investigated, we highlight the importance of using independent evidence for localization as a prerequisite for understanding physiological function of membrane proteins.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Fuchs, P., Feixes-Prats, E., Arruda, P., Feitosa-Araújo, E., Fernie, A. R., Grefen, C., Lichtenauer, S., Linka, N., de Godoy Maia, I., Meyer, A. J., Schilasky, S., Sweetlove, L. J., Wege, S., Weber, A. P., Millar, A. H., Keech, O., Florez Sarasa, I., Barreto, P., & Schwarzländer, M.
- Affiliations
- University of Bonn (DE)
- Universitat Autònoma de Barcelona (ES)
- Universidade Estadual de Campinas (UNICAMP) (BR)
- Max Planck Society (DE)
- Ruhr University Bochum (DE)
- University of Münster (DE)
- Cluster of Excellence on Plant Sciences (DE)
- University of Oxford (GB)
- The University of Western Australia (AU)
- Umeå Plant Science Centre (SE)
- Corresponding author
- Barreto, Pedro
- Schwarzländer, Markus
- ORCID
- Fuchs, Philippe
- Feixes-Prats, Elisenda
- Arruda, Paulo
- Feitosa-Araújo, Elias
- Fernie, Alisdair R.
- Grefen, Christopher
- Lichtenauer, Sophie
- Linka, Nicole
- Meyer, Andreas J.
- Schilasky, Sören
- Sweetlove, Lee J.
- Wege, Stefanie
- Weber, Andreas P.
- Millar, A. Harvey
- Keech, Olivier
- Florez Sarasa, Igor
- Barreto, Pedro
- Schwarzländer, Markus
- Venue
- PLANT PHYSIOLOGY
- Publisher
- openRxiv
- Published
- 2023-05-08
- Volume
- 194
- Issue
- 2
- Pages
- 623-628
- ISSN
- 0032-0889 (ISSN-L)
- OpenAlex
- W4387520759
- Cited by
- 3
- References
- 1
- Citations by year
- 2025: 1 · 2024: 2
- FWCI
- 0.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- PLANT PHYSIOLOGY (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (publishedVersion, other-oa)
- UWA Profiles and Research Repository (UWA) (submittedVersion, other-oa)
- HAL (submittedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- IRTA (Institut de Recerca i Tecnologia Agroalimentaries) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SCHW 1719/9-1, MCIN /AEI/10.13039/501100011033, GRK2064)
- Conselho Nacional de Desenvolvimento Científico e Tecnológico (MCIN/AEI/10.13039/501100011033, AEI/10.13039/501100011033)
- Westfälische Wilhelms-Universität Münster (RI_00497)
- Agencia Estatal de Investigación (AEI//10.13039/501100011033/, 501100011033, 10.13039/501100011033, MCIN/AEI/10.13039/501 100 011 033, 13039, .13039/501100011033, 10.13039, AEI/10)
- European Social Fund (MCIN/AEI/10.13039/ 501100011033, 501100011033, AEI/10.13039/501100011033)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- UCP2, Golgi apparatus, protein localization, UCP1, mitochondrial carrier protein, plant mitochondria
- MeSH terms
- Golgi Apparatus, Humans, Membrane Proteins, Mitochondrial Proteins
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