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. STKE, 30 April 2002
Vol. 2002, Issue 130, p. tw159
[DOI: 10.1126/stke.2002.130.tw159]


Cell Biology PKC{varepsilon} Moved to the Membrane by Tyrosine Nitration

Modification of proteins by covalent attachment of NO groups has emerged as an important mechanism for the regulation of signaling. In addition, drugs that produce reactive NO species are well-known agents used during cardiac ischemic episodes. Balafanova et al. show that tyrosine nitration of protein kinase C{varepsilon} (PKC{varepsilon}) stimulates PKC{varepsilon} catalytic activity by promoting its interaction with receptor for activated protein kinase C2 (RACK2), and, thus, its translocation to the membranes of cardiomyocytes. This elucidates a mechanism by which NO can stimulate PKC{varepsilon} activity.

Z. Balafanova, R. Bolli, J. Zhang, Y. Zheng, J. M. Pass, A. Bhatnagar, X.-L. Tang, O. Wang, E. Cardwell, P. Ping, Nitric oxide (NO) induces nitration of protein kinase C{varepsilon} (PKC{varepsilon}), facilitating PKC{varepsilon} translocation via enhanced PKC{varepsilon}-RACK2 interactions: A novel mechanism of NO-triggered activation of PKC{varepsilon}. J. Biol. Chem. 277, 15021-15027 (2002). [Abstract] [Full Text]

Citation: PKC{varepsilon} Moved to the Membrane by Tyrosine Nitration. Sci. STKE 2002, tw159 (2002).

To Advertise     Find Products

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