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.
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Acknowledgments
The author thanks other laboratory members for critical reading of this manuscript. This study was supported by NIH Grants (CA169186) to YJ. The author has no conflict of interest to declare for this publication.
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Communicated by M. Kupiec.
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Jiang, Y. Regulation of TORC1 by ubiquitin through non-covalent binding. Curr Genet 62, 553–555 (2016). https://doi.org/10.1007/s00294-016-0581-7
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DOI: https://doi.org/10.1007/s00294-016-0581-7