Reference: Ahuja N, et al. (2007) Regulation of Insulin Secretion by SIRT4, a Mitochondrial ADP-ribosyltransferase. J Biol Chem 282(46):33583-92

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Abstract


Sirtuins are homologues of the yeast transcriptional repressor Sir2p and are conserved from bacteria to hu-mans. We report that human SIRT4 is localized to the mitochondria. SIRT4 is a matrix protein and becomes cleaved at amino acid 28 after import into mito-chondria. Mass spectrometry analysis of proteins that coimmunoprecipitate with SIRT4 identified insulin-degrading enzyme and the ADP/ATP carrier proteins, ANT2 and ANT3. SIRT4 exhibits no histone deacetylase activity but functions as an efficient ADP-ribosyltransferase on histones and bovine serum albumin. SIRT4 is expressed in islets of Langerhans, and colocalizes with insulin-expressing b cells. Depletion of SIRT4 from insulin-producing INS-1E cells results in increased insulin secretion in response to glucose. These observations define a new role for mitochondrial SIRT4 in the regulation of insulin secretion.

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Journal Article
Authors
Ahuja N, Schwer B, Carobbio S, Waltregny D, North BJ, Castronovo V, Maechler P, Verdin E
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