Journal article

Protein hypoacylation induced by Sirt5 overexpression has minimal metabolic effect in mice

Nicholas L Bentley, Corrine E Fiveash, Brenna Osborne, Lake-Ee Quek, Masahito Ogura, Nobuya Inagaki, Gregory J Cooney, Patsie Polly, Magdalene K Montgomery, Nigel Turner

Biochemical and Biophysical Research Communications | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2018

Abstract

Sirtuins are a family of evolutionary conserved enzymes that dynamically regulate cellular physiology. Mammals have 7 sirtuins, which are located in different cellular compartments. Sirt5, a sirtuin isoform located in multiple subcellular sites, is involved in regulating a diverse range of cellular and metabolic processes through the removal of a range of acyl-lysine modifications on target proteins. Loss of Sirt5 leads to hyper-malonylation and hyper-succinylation of both mitochondrial and extra-mitochondrial proteins, influencing oxidative phosphorylation, the TCA cycle and glycolysis. However despite these findings, the effect of Sirt5 overexpression on metabolism remains poorly investiga..

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University of Melbourne Researchers

Grants

Awarded by National Health and Medical Research Council of Australia (NHMRC)


Awarded by Australian Research Council


Funding Acknowledgements

This work was supported by funding from the National Health and Medical Research Council of Australia (NHMRC; APP1043779), the Australian Research Council (FT120100371) and the Diabetes Australia Research Trust. NLB was supported by an Australian Postgraduate Award Scholarship and MKM is supported by a NHMRC Career Development Fellowship. Animal work was made possible thanks to kind staff in the UNSW BRC.