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A degron is a portion of a protein that is important in regulation of protein degradation rates. Known degrons include short amino acid sequences, structural motifs and exposed amino acids located anywhere in the protein. In fact, some proteins can even contain multiple degrons. Degrons are present in a variety of organisms, from the N-degrons first characterized in yeast to the PEST sequence of mouse ornithine decarboxylase. Degrons have been identified in prokaryotes as well as eukaryotes. While there are many types of different degrons, and a high degree of variability even within these groups, degrons are all similar for their involvement in regulating the rate of a protein's degradation. Much like protein degradation mechanisms are categorized by their dependence or lack thereof on Ubiquitin, a small protein involved in proteasomal protein degradation, Degrons may also be referred to as “Ubiquitin-dependent" or “Ubiquitin-independent".
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References
- ↑ Rogers S, Wells R, Rechsteiner M (1986). "Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis". Science . 234 (4774): 364–8. Bibcode:1986Sci...234..364R. doi:10.1126/science.2876518. PMID 2876518.
- ↑ Reverte CG, Ahearn MD, Hake LE (2001). "CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome". Dev. Biol. 231 (2): 447–58. doi: 10.1006/dbio.2001.0153 . PMID 11237472.
- ↑ Spencer ML, Theodosiou M, Noonan DJ (2004). "NPDC-1, a novel regulator of neuronal proliferation, is degraded by the ubiquitin/proteasome system through a PEST degradation motif". J. Biol. Chem. 279 (35): 37069–78. doi: 10.1074/jbc.M402507200 . PMID 15229225.
- ↑ Shumway SD, Maki M, Miyamoto S (1999). "The PEST Domain of IκBα is necessary and sufficient for in vitro degradation by mu-calpain". J. Biol. Chem. 274 (43): 30874–81. doi: 10.1074/jbc.274.43.30874 . PMID 10521480.
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