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Sci. Signal., 23 February 2010
Vol. 3, Issue 110, p. ec60
[DOI: 10.1126/scisignal.3110ec60]

EDITORS' CHOICE

Protein Turnover To Degrade or Not to Degrade

Stella M. Hurtley

Science, AAAS, Cambridge CB2 1LQ, UK

Regulating the turnover of proteins within the cell is of fundamental importance to almost every physiological process. Hwang et al. (see the Perspective by Mogk and Bukau) now find that acetylated N-terminal methionine (Met) is a degradation signal. This degron is recognized by Saccharomyces cerevisiae Doa10, a transmembrane E3 ubiquitin ligase that resides in the endoplasmic reticulum and inner nuclear membrane. The removal of N-terminal Met by Met-aminopeptidases generates N-terminal residues that are often N-terminally acetylated. Doa10 selectively binds to the resulting N-degrons, which may represent the most prevalent class of cellular protein degradation signals.

C.-S. Hwang, A. Shemorry, A. Varshavsky, N-terminal acetylation of cellular proteins creates specific degradation signals. Science 327, 973–977 (2010). [Abstract] [Full Text]

A. Mogk, B. Bukau, When the beginning marks the end. Science 327, 966–967 (2010). [Summary] [Full Text]

Citation: S. M. Hurtley, To Degrade or Not to Degrade. Sci. Signal. 3, ec60 (2010).


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