Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 22, Issue 7, Pages -Publisher
MDPI
DOI: 10.3390/ijms22073545
Keywords
N-degron; ubiquitin proteasome pathway; autophagy; protein turnover; proteolytic processing; endoprotease
Funding
- Austrian Science Fund FWF [P31114, F7904-B]
- Austrian Science Fund (FWF) [P31114] Funding Source: Austrian Science Fund (FWF)
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The first amino acid of a protein plays a significant role in its metabolic stability, with N-degrons mediating turnover. Despite only a few proteases known to contribute to the generation of N-degrons, there is potential for further discovery in many processing paths.
The first amino acid of a protein has an important influence on its metabolic stability. A number of ubiquitin ligases contain binding domains for different amino-terminal residues of their substrates, also known as N-degrons, thereby mediating turnover. This review summarizes, in an exemplary way, both older and more recent findings that unveil how destabilizing amino termini are generated. In most cases, a step of proteolytic cleavage is involved. Among the over 500 proteases encoded in the genome of higher eukaryotes, only a few are known to contribute to the generation of N-degrons. It can, therefore, be expected that many processing paths remain to be discovered.
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