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N-end rule of selective protein turnover: mechanistic aspects and functional implications

Varshavsky, Alexander and Bachmair, Andreas and Finley, Daniel (1987) N-end rule of selective protein turnover: mechanistic aspects and functional implications. Biochemical Society Transactions, 15 (5). pp. 815-816. ISSN 0300-5127. https://resolver.caltech.edu/CaltechAUTHORS:20201201-103332052

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Abstract

In both bacterial and eukaryotic cells, relatively long-lived proteins, whose half-lives are close to or exceed the cell generation time, coexist with proteins whose half-lives can be less than 1% of the cell generation time. Rates of intra-cellular protein degeneration are a function of the cell’s physiological state, and appear to be controlled differentially for individual proteins. In particular, damaged and some otherwise abnormal proteins are metabolically unstable in vivo. Although the specific functions of selective protein degradation are in most cases still unknown, it is clear that many regulatory proteins are extremely short-lived in vivo. Metabolic instability of such proteins allows for rapid adjustments of their intracellular concentrations through regulated changes in rates of their synthesis or degradation.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1042/bst0150815DOIArticle
ORCID:
AuthorORCID
Varshavsky, Alexander0000-0002-4011-258X
Additional Information:© 1987 Biochemical Society.
Issue or Number:5
Record Number:CaltechAUTHORS:20201201-103332052
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20201201-103332052
Official Citation:ALEXANDER VARSHAVSKY, ANDREAS BACHMAIR, DANIEL FINLEY; The N-end rule of selective protein turnover: mechanistic aspects and functional implications. Biochem Soc Trans 1 October 1987; 15 (5): 815–816. doi: https://doi.org/10.1042/bst0150815
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:106860
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:02 Dec 2020 17:21
Last Modified:02 Dec 2020 17:21

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