Sirtuin-3 deacetylation of cyclophilin D induces dissociation of hexokinase II from the mitochondria

Year: 2010

Type: article

Abstract: 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.

Source: Journal of Cell Science

DOI: 10.1242/jcs.061846

Authors: Nataly Shulga, Robin Wilson-Smith, John G. Pastorino

Institutions: University of Medicine and Dentistry of New Jersey, Cooper University Hospital

Language: English

Topic: Sirtuins and Resveratrol in Medicine

Subfield: Geriatrics and Gerontology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funder: National Cancer Institute