Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. Signal., 27 May 2008
Vol. 1, Issue 21, p. ec202
[DOI: 10.1126/stke.121ec202]

EDITORS' CHOICE

Cell Biology Regulating S-Nitrosylation

L. Bryan Ray

Science, Science Signaling, AAAS, Washington, DC 20005, USA

Covalent modification of proteins by S-nitrosylation is an important mechanism for regulation of biochemical activity in cells. However, mechanisms of protein denitrosylation have not been well characterized. The protease caspase-3, which promotes apoptosis, is inhibited by S-nitrosylation and is denitrosylated in cells in which the cell death-promoting receptor Fas is activated. Benhar et al. (see the Perspective by Holmgren) purified a protein fraction that catalyzed denitrosylation of caspase-3 and identified thioredoxin-1 (Trx1) as the protein most likely to be responsible for the denitrosylation activity. Depletion of Trx1 caused accumulation of S-nitrosylated caspase-3 and other S-nitrosylated proteins in cultured cells, and Fas-induced denitrosylation of caspase-3 was inhibited by depleting thioredoxin reductase 2. Thus, regulated denitrosylation of target proteins by Trx1 appears to provide a key component of enzymatic regulation of caspase-3 and possibly other proteins by S-nitrosylation.

M. Benhar, M. T. Forrester, D. T. Hess, J. S. Stamler, Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320, 1050-1054 (2008). [Abstract] [Full Text]

A. Holmgren, SNO Removal. Science 320, 1019-1020 (2008). [Summary] [Full Text]

Citation: L. B. Ray, Regulating S-Nitrosylation. Sci. Signal. 1, ec202 (2008).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882