{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shemorry A"],"funding":["NIDDK NIH HHS","NIGMS NIH HHS"],"pagination":["540-51"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3665649"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["50(4)"],"pubmed_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 th"],"journal":["Molecular cell"],"pubmed_title":["Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway."],"pmcid":["PMC3665649"],"funding_grant_id":["R56 DK039520","DK039520","R01 GM031530","R01 DK039520","GM031530","R01 GM085371","R37 DK039520","GM085371"],"pubmed_authors":["Varshavsky A","Shemorry A","Hwang CS"],"additional_accession":[]},"is_claimable":false,"name":"Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway.","description":"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 th","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 May","modification":"2025-04-04T23:39:39.116Z","creation":"2019-03-27T01:10:29Z"},"accession":"S-EPMC3665649","cross_references":{"pubmed":["23603116"],"doi":["10.1016/j.molcel.2013.03.018"]}}