Degrade to create: developmental requirements for ubiquitin-mediated proteolysis during earlyC. elegansembryogenesis

Author:

Bowerman Bruce1,Kurz Thimo2

Affiliation:

1. Institute of Molecular Biology, University of Oregon, Eugene, OR 97403,USA.

2. Institute of Biochemistry, ETH Zürich, Hönggerberg, 8093 Zürich, Switzerland.

Abstract

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.

Publisher

The Company of Biologists

Subject

Developmental Biology,Molecular Biology

Reference110 articles.

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3. Amon, A. (1999). The spindle checkpoint. Curr. Opin. Genet. Dev.9, 69-75.

4. Ang, X. L. and Harper, J. W. (2004). Interwoven ubiquitination oscillators and control of cell cycle transitions. Sci. STKE2004,pe31.

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