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First published online February 9, 2006
doi: 10.1242/10.1242/dev.02276

Development 133, 773-784 (2006)
Published by The Company of Biologists 2006
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Review

Degrade to create: developmental requirements for ubiquitin-mediated proteolysis during early C. elegans embryogenesis

Bruce Bowerman1 and Thimo Kurz2,*

1 Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
2 Institute of Biochemistry, ETH Zürich, Hönggerberg, 8093 Zürich, Switzerland.

* Author for correspondence (e-mail: thimo.kurz{at}bc.biol.ethz.ch)

SUMMARY

The ubiquitin protein conjugation system tags proteins with the small polypeptide ubiquitin. Most poly-ubiquitinated proteins are recognized and degraded by the proteasome, a large multi-subunit protease. Ubiquitin-dependent protein degradation is used as a regulatory tool for many essential processes, the best studied of which is eukaryotic cell cycle progression. More recently, genetic studies in C. elegans have identified multiple roles for the ubiquitin system in early development, where ubiquitin-dependent protein degradation governs such diverse events as passage through meiosis, cytoskeletal regulation and cell fate determination.




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