Degradation signal diversity in the ubiquitin-proteasome system
By T. Ravid, M. Hochstrasser. Nature reviews. Molecular cell biology, 2008
808 citations recorded by the source corpus.
The 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.
Subfields: Cancer Research, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/ecc8ff41feac93b7bc2472d7b8771af9ed8d0a94
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In Molecular Biology
Citations in the corpus
- Sequence signatures and mRNA concentration can explain two-thirds of protein abundance variation in a human cell line (2010, background): “Sequence signatures and mRNA concentration can explain two-thirds of protein abundance variation in a human cell line Christine Vogel1,5,*, Raquel de Sousa Abreu2,5, Daijin Ko3, Shu-Yun Le4, Bruce A Shapiro4, Suzanne C Burns2, Devraj Sandhu2, Daniel R Boutz1, Edward M Marcotte1 and Luiz O Penalva2,*”
- High-throughput Analysis of in vivo Protein Stability* (2013, methodology): “We demonstrate the Stable-seq method by the analysis of a degron, which is a protein degradation signal recognized by the proteolytic machinery (6).”