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KMID : 0620920180500070091
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Experimental & Molecular Medicine
2018 Volume.50 No. 7 p.91 ~ p.91
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Control of protein degradation by N-terminal acetylation and the N-end rule pathway
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Nguyen Kha The
Mun Sang-Hyeon
Lee Chang-Seok
Hwang Cheol-Sang
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Abstract
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Nα-terminal acetylation (Nt-acetylation) occurs very frequently and is found in most proteins in eukaryotes. Despite the pervasiveness and universality of Nt-acetylation, its general functions in terms of physiological outcomes remain largely elusive. However, several recent studies have revealed that Nt-acetylation has a significant impact on protein stability, activity, folding patterns, cellular localization, etc. In addition, Nt-acetylation marks specific proteins for degradation by a branch of the N-end rule pathway, a subset of the ubiquitin-mediated proteolytic system. The N-end rule associates a protein’s in vivo half-life with its N-terminal residue or modifications on its N-terminus. This review provides a current understanding of intracellular proteolysis control by Nt-acetylation and the N-end rule pathway.
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KEYWORD
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Protein folding
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