PerspectiveCell Biology

An Ancient Portal to Proteolysis

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Science  17 Aug 2012:
Vol. 337, Issue 6096, pp. 813-814
DOI: 10.1126/science.1227301

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Summary

Selective protein degradation in eukaryotes is mediated primarily by the ubiquitin-proteasome system, in which the small protein ubiquitin is covalently attached to a target protein to signal its degradation by the 26S proteasome (1). The ubiquitin-proteasome system may include as many as 1000 distinct gene products, thus constituting one of the broadest regulatory systems in nature. Recent work, including a report by Barthelme and Sauer on page 843 of this issue (2), has shed light on how this baroque pathway may have evolved and raises some unexpected possibilities for the mechanism by which proteins are delivered to proteasomes for their destruction.