title: Regulation of TORC1 by ubiquitin through non-covalent binding.
abstract: Ubiquitin (Ub) regulates numerous cellular processes through covalent attachment to other proteins in the forms of poly- and mono-ubiquitination. A recent study in yeast shows that ubiquitin controls TORC1 through a noncovalent binding with Kog1, a regulatory subunit of TORC1. The binding stabilizes Kog1 and prevents its degradation under stress conditions. This finding unveils a novel role of Ub in TORC1 function and implicates a unique mechanism that attributes the action of Ub in cell signaling.
authors.affiliation: Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15213, USA. yuj5@pitt.edu.
authors.forename: Yu
authors.initials: Y
authors.lastname: Jiang
mesh_terms: D000076222:Mechanistic Target of Rapamycin Complex 1; D046912:Multiprotein Complexes / Q000378:metabolism*; D011485:Protein Binding; D015398:Signal Transduction; D058570:TOR Serine-Threonine Kinases / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D046912:Multiprotein Complexes; D025801:Ubiquitin; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases
keywords: Kog1; Rapamycin; TOR; Ubiquitin; WD40 repeats