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, 9 July 2002
Vol. 2002, Issue 140, p. tw242
[DOI: 10.1126/stke.2002.140.tw242]

EDITORS' CHOICE

Protein Modifications Taking Degradation to Heart

The ubiquitin pathway of protein degradation has gained prominence as a major regulatory network in mammalian cells. Arginine is commonly conjugated to the NH2-terminus of proteins during ubiquitin-dependent degradation, but the physiological functions of arginylation are unknown. Kwon et al. generated mice genetically deficient in one of the Arg-tRNA-protein transferases catalyzing this modification (ATE-1) and found that the embryos die from defects in heart development and angiogenesis. The authors also discovered a possible mechanism for the early cardiac defects: NH2-terminal cysteine is oxidized prior to its arginylation by ATE-1, suggesting that the NH2-terminal arginylation may function as an oxygen sensor.

Y. T. Kwon, A. S. Kashina, I. V. Davydov, R.-G. Hu, J. Y. An, J. W. Seo, F. Du, A. Varshavsky, An essential role of N-terminal arginylation in cardiovascular development. Science 296, 96-99 (2002). [Abstract] [Full Text]

Citation: Taking Degradation to Heart. Sci. STKE 2002, tw242 (2002).


To Advertise     Find Products


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