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 Diversity of degradation signals in the ubiquitin-proteasome system Ravid T; Hochstrasser MNat Rev Mol Cell Biol  2008[Sep]; 9 (9): 679-90The ubiquitin-proteasome system degrades an enormous variety of proteins that  contain specific degradation signals, or 'degrons'. Besides the degradation of  regulatory proteins, almost every protein suffers from sporadic biosynthetic  errors or misfolding. Such aberrant proteins can be recognized and rapidly  degraded by cells. Structural and functional data on a handful of degrons allow  several generalizations regarding their mechanism of action. We focus on  different strategies of degron recognition by the ubiquitin system, and contrast  regulatory degrons that are subject to signalling-dependent modification with  those that are controlled by protein folding or assembly, as frequently occurs  during protein quality control.|*Protein Processing, Post-Translational[MESH]|*Signal Transduction[MESH]|Animals[MESH]|Endoplasmic Reticulum/metabolism[MESH]|Humans[MESH]|Proteasome Endopeptidase Complex/*metabolism[MESH]|Ubiquitin-Protein Ligases/metabolism[MESH]|Ubiquitin/*metabolism[MESH]
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