Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 81
Volume 81, Issue -, Pages 261-289Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-051710-093308
Keywords
N-degron; arginylation; ubiquitin; proteolysis
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Funding
- NCATS NIH HHS [UL1 TR000005] Funding Source: Medline
- NHLBI NIH HHS [HL083365, R01 HL083365] Funding Source: Medline
- NATIONAL CENTER FOR ADVANCING TRANSLATIONAL SCIENCES [UL1TR000005] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL083365] Funding Source: NIH RePORTER
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The N-end rule pathway is a proteolytic system in which N-terminal residues of short-lived proteins are recognized by recognition components (N-recognins) as essential components of degrons, called N-degrons. Known N-recognins in eukaryotes mediate protein ubiquitylation and selective proteolysis by the 26S proteasome. Substrates of N-recognins can be generated when normally embedded destabilizing residues are exposed at the N terminus by proteolytic cleavage. N-degrons can also be generated through modifications of posttranslationally exposed pro-N-degrons of otherwise stable proteins; such modifications include oxidation, arginylation, leucylation, phenylalanylation, and acetylation. Although there are variations in components, degrons, and hierarchical structures, the proteolytic systems based on generation and recognition of N-degrons have been observed in all eukaryotes and prokaryotes examined thus far. The N-end rule pathway regulates homeostasis of various physiological processes, in part, through interaction with small molecules. Here, we review the biochemical mechanisms, structures, physiological functions, and small-molecule-mediated regulation of the N-end rule pathway.
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