Cellular Control of Protein Turnover via the Modification of the Amino Terminus.

Nikola Winter, Maria Novatchkova, Andreas Bachmair

Journal: International journal of molecular sciences 2021;22(7):3545

PMID: 33805528

Abstract

["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."]

Address: Max Perutz Labs, Department of Biochemistry and Cell Biology, University of Vienna, A-1030 Vienna, Austria.; Vienna BioCenter, Research Institute of Molecular Pathology, A-1030 Vienna, Austria.; Vienna BioCenter, Institute of Molecular Biotechnology, A-1030 Vienna, Austria.

DOI: 10.3390/ijms22073545

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MeSH Terms: Bacterial Proteins, Caspases, Endopeptidases, Endoplasmic Reticulum, Humans, Methionyl Aminopeptidases, Protein Sorting Signals, Proteins, Proteolysis, Ribosomes, Ubiquitin-Protein Ligases