期刊
LYSINE-BASED POST-TRANSLATIONAL MODIFICATION OF PROTEINS
卷 52, 期 -, 页码 23-35出版社
PORTLAND PRESS LTD
DOI: 10.1042/BSE0520023
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资金
- NIDDK NIH HHS [R24 DK085610] Funding Source: Medline
Changes in cellular nutrient availability or energy status induce global changes in mitochondrial protein acetylation. Over one-third of all proteins in the mitochondria are acetylated, of which the majority are involved in some aspect of energy metabolism. Mitochondrial protein acetylation is regulated by SIRT3 (sirtuin 3), a member of the sirtuin family of NAD(+)-dependent protein deacetylases that has recently been identified as a key modulator of energy homoeostasis. In the absence of SIRT3, mitochondrial proteins become hyperacetylated, have altered function, and contribute to mitochondrial dysfunction. This chapter presents a review of the functional impact of mitochondrial protein acetylation, and its regulation by SIRT3.
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