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Nature Cell Biology 6, 571 - 572 (2004)
doi:10.1038/ncb0704-571
Ubiquitin signalling: what's in a chain?
Mark Hochstrasser1
- Mark Hochstrasser is in the Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, New Haven, CT 06520-8114, USA. e-mail: mark.hochstrasser@yale.edu
Abstract
When cellular proteins are attached to a Lys 48-linked polyubiquitin chain, the proteasome will usually degrade them. But attaching such a chain to a yeast transcription factor inhibits its activity without degradation, raising questions about how polyubiquitination regulates transcriptional activation and why the protein is spared destruction.
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