Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway
SCIE
SCOPUS
- Title
- Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway
- Authors
- Shemorry, A; Hwang, CS; Varshavsky, A
- Date Issued
- 2013-05-23
- Publisher
- Cell Press
- Abstract
- N-alpha-terminal acetylation of cellular proteins was recently discovered to create specific degradation signals termed Ac/N-degrons and targeted by the Ac/N-end rule pathway. We show that Hcn1, a subunit of the APC/C ubiquitin ligase, contains an Ac/N-degron that is repressed by Cut9, another APC/C subunit and the ligand of Hcn1. Cog1, a subunit of the Golgi-associated COG complex, is also shown to contain an Ac/N-degron. Cog2 and Cog3, direct ligands of Cog1, can repress this degron. The subunit decoy technique was used to show that the long-lived endogenous Cog1 is destabilized and destroyed via its activated (unshielded) Ac/N-degron if the total level of Cog1 increased in a cell. Hurl and Cog1 are the first examples of protein regulation through the physiologically relevant transitions that shield and unshield natural Ac/N-degrons. This mechanistically straightforward circuit can employ the demonstrated conditionality of Ac/N-degrons to regulate subunit stoichiometries and other aspects of protein quality control.
- Keywords
- UBIQUITIN-PROTEASOME SYSTEM; DEGRADATION SIGNALS; COMPLEX; YEAST; ACETYLTRANSFERASES; SUBUNIT; RECOGNITION; PROTEOLYSIS; EXPRESSION; RIBOSOME
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/14997
- DOI
- 10.1016/J.MOLCEL.2013.03.018
- ISSN
- 1097-2765
- Article Type
- Article
- Citation
- Molecular Cell, vol. 50, no. 4, page. 540 - 551, 2013-05-23
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