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

Medienart:

E-Artikel

Erscheinungsjahr:

2010

Erschienen:

2010

Enthalten in:

Zur Gesamtaufnahme - volume:123

Enthalten in:

Journal of cell science - 123(2010), Pt 6 vom: 15. März, Seite 894-902

Sprache:

Englisch

Beteiligte Personen:

Shulga, Nataly [VerfasserIn]
Wilson-Smith, Robin [VerfasserIn]
Pastorino, John G [VerfasserIn]

Links:

Volltext

Themen:

Adenine Nucleotide Translocator 1
Culture Media
Cyclophilins
EC 2.7.1.1
EC 3.5.1.-
EC 5.2.1.-
Galactose
Hexokinase
Journal Article
K3Z4F929H6
Lysine
Mitochondrial Proteins
Peptidyl-Prolyl Isomerase F
Research Support, N.I.H., Extramural
Retracted Publication
SIRT3 protein, human
SIRT4 protein, human
SIRT5 protein, human
Sirtuin 3
Sirtuins
X2RN3Q8DNE

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

doi:

10.1242/jcs.061846

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM195135717