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Mol Cell. 2013 May 23;50(4):540-51. doi: 10.1016/j.molcel.2013.03.018. Epub 2013 Apr 18.

Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway.

Author information

1
Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.

Abstract

N(α)-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. Hcn1 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.

PMID:
23603116
PMCID:
PMC3665649
DOI:
10.1016/j.molcel.2013.03.018
[Indexed for MEDLINE]
Free PMC Article

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