Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria
We demonstrate that the transition from a reliance on glycolysis to oxidative phosphorylation in a transformed cell line is dependent on an increase in the levels and activity of sirtuin-3. Sirtuin-3 deacetylates cyclophilin D, diminishing its peptidyl-prolyl cis-trans isomerase activity and inducing its dissociation from the adenine nucleotide translocator. Moreover, the sirtuin-3-induced inactivation of cyclophilin D causes a detachment of hexokinase II from the mitochondria that is necessary for stimulation of oxidative phosphorylation. These results might have important implications for the role of sirtuin-3 in the metabolism of some cancer cells and their susceptibility to mitochondrial injury and cytotoxicity.
Errataetall: |
ExpressionOfConcernIn: J Cell Sci. 2016 Feb 15;129(4):868. - PMID 26905965 |
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Medienart: |
E-Artikel |
Erscheinungsjahr: |
2010 |
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Erschienen: |
2010 |
Enthalten in: |
Zur Gesamtaufnahme - volume:123 |
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Enthalten in: |
Journal of cell science - 123(2010), Pt 6 vom: 15. März, Seite 894-902 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Shulga, Nataly [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 15.06.2010 Date Revised 13.12.2023 published: Print-Electronic ExpressionOfConcernIn: J Cell Sci. 2016 Feb 15;129(4):868. - PMID 26905965 Citation Status MEDLINE |
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doi: |
10.1242/jcs.061846 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM195135717 |
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520 | |a We demonstrate that the transition from a reliance on glycolysis to oxidative phosphorylation in a transformed cell line is dependent on an increase in the levels and activity of sirtuin-3. Sirtuin-3 deacetylates cyclophilin D, diminishing its peptidyl-prolyl cis-trans isomerase activity and inducing its dissociation from the adenine nucleotide translocator. Moreover, the sirtuin-3-induced inactivation of cyclophilin D causes a detachment of hexokinase II from the mitochondria that is necessary for stimulation of oxidative phosphorylation. These results might have important implications for the role of sirtuin-3 in the metabolism of some cancer cells and their susceptibility to mitochondrial injury and cytotoxicity | ||
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