SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine

Hong Jiang, Saba Khan, Yi Wang, Guillaume Charron, Bin He, Carlos Sebastian, Jintang Du, Ray Kim, Eva Ge, Raul Mostoslavsky, Howard C. Hang, Quan Hao () and Hening Lin ()
Additional contact information
Hong Jiang: Cornell University
Saba Khan: Cornell University
Yi Wang: University of Hong Kong
Guillaume Charron: The Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
Bin He: Cornell University
Carlos Sebastian: The Massachusetts General Hospital Cancer Center, Harvard Medical School, 185 Cambridge St., Boston, Massachusetts 02114, USA
Jintang Du: Cornell University
Ray Kim: Cornell University
Eva Ge: Cornell University
Raul Mostoslavsky: The Massachusetts General Hospital Cancer Center, Harvard Medical School, 185 Cambridge St., Boston, Massachusetts 02114, USA
Howard C. Hang: The Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
Quan Hao: University of Hong Kong
Hening Lin: Cornell University

Nature, 2013, vol. 496, issue 7443, 110-113

Abstract: The sirtuin family of enzymes are known as NAD-dependent deacetylases, although some of them have very weak deacetylase activity; here human SIRT6, an enzyme important for DNA repair and transcription, is shown to remove long-chain fatty acyl groups from protein lysine residues, and to have a function in promoting tumour necrosis factor alpha secretion.

Date: 2013
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DOI: 10.1038/nature12038

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