Editors' ChoiceCell Biology

PKCε Moved to the Membrane by Tyrosine Nitration

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Science's STKE  30 Apr 2002:
Vol. 2002, Issue 130, pp. tw159
DOI: 10.1126/stke.2002.130.tw159

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 Cε (PKCε) stimulates PKCε 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 PKCε 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 Cε (PKCε), facilitating PKCε translocation via enhanced PKCε-RACK2 interactions: A novel mechanism of NO-triggered activation of PKCε. J. Biol. Chem. 277, 15021-15027 (2002). [Abstract] [Full Text]

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