Amino Acid Signaling to mTOR Mediated by Inositol Polyphosphate Multikinase
| Autor: | Seung Hun Cha, Roxanne K. Barrow, David Maag, Adele M. Snowman, Anutosh Chakraborty, Adam C. Resnick, Michael A. Koldobskiy, Seyun Kim, Krishna R. Juluri, Solomon H. Snyder, Sangwon F. Kim, Micah J. Maxwell |
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| Rok vydání: | 2011 |
| Předmět: |
Physiology
mTORC1 Biology mTORC2 Article Cell Line Mice 03 medical and health sciences 0302 clinical medicine Animals Humans Amino Acids Inositol phosphate Molecular Biology PI3K/AKT/mTOR pathway 030304 developmental biology chemistry.chemical_classification 0303 health sciences TOR Serine-Threonine Kinases RPTOR Cell Biology Fibroblasts Amino acid Phosphotransferases (Alcohol Group Acceptor) Amino Acid Substitution chemistry Biochemistry 030220 oncology & carcinogenesis Mutation Biocatalysis biological phenomena cell phenomena and immunity Signal transduction Protein Binding Signal Transduction |
| Zdroj: | Cell Metabolism. 13:215-221 |
| ISSN: | 1550-4131 |
| DOI: | 10.1016/j.cmet.2011.01.007 |
| Popis: | SummarymTOR complex 1 (mTORC1; mammalian target of rapamycin [mTOR] in complex with raptor) is a key regulator of protein synthesis and cell growth in response to nutrient amino acids. Here we report that inositol polyphosphate multikinase (IPMK), which possesses both inositol phosphate kinase and lipid kinase activities, regulates amino acid signaling to mTORC1. This regulation is independent of IPMK's catalytic function, instead reflecting its binding with mTOR and raptor, which maintains the mTOR-raptor association. Thus, IPMK appears to be a physiologic mTOR cofactor, serving as a determinant of mTORC1 stability and amino acid-induced mTOR signaling. Substances that block IPMK-mTORC1 binding may afford therapeutic benefit in nutrient amino acid-regulated conditions such as obesity and diabetes. |
| Databáze: | OpenAIRE |
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