GLY-934 ОБЕСПЕЧИВАЕТ ВЗАИМОДЕЙСТВИЕ РИКТОРА С SIN1
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Keywords:
mTOR, kinase,Abstract
mTOR (mammalian target of rapamycin) is an important hub kinase of growth factor and nutrient signaling. Functioning as a part of two distinct multiprotein complexes - mTORC1 and mTORC2 (mTOR complexes 1 and 2) – it regulates cell growth and proliferation. We have established that Gly-934 residue of mTORC2’s rictor plays a key role in maintaining rictor-Sin1 interaction.References
1. Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control // Mol Cell. - 2002. - Vol.10. - P.457–468.
2. Chen C.-H., Shaikenov T., Aimbetov R., Peterson T.R., Bissenbaev A.K., Lee S.-W., Wu J., Lin H.-K., Sarbassov D.D. ER stress inhibits mTORC2 and Akt signaling through GSK-3β-mediated phosphorylation of rictor // Science Signaling. - 2011. -Vol.4(161). - P.ra10.
3. Kannan N., Haste N., Taylor S.S., Neuwald A.F. The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module // Proc Natl Acad Sci USA. - 2007. - Vol.104(4). - P.1272-7.
4. Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex // Science. - 2005. - Vol.307. - P.1098–1101.
5. Jones K.T., Greer E.R., Pearce D., Ashrafi K. Rictor/TORC2 regulates Caenorhabditis elegans fat storage, body size, and development through sgk-1 // PLoS Biol. - 2009. - Vol.7. - P.0604-0615.
6. Soukas A.A., Kane E.A., Carr C.E., Melo J.A., Ruvkun G. Rictor/TORC2 regulates fat metabolism, feeding, growth, and life span in Caenorhabditis elegans // Genes Dev. - 2009. - Vol.23. - P.496-511.
7. Sarbassov D.D., Ali S.M., Kim D.H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton // Curr Biol. - 2004. - Vol.14. - P.1296–1302.
8. Martín de Llano J.J., Fuertes G., Andreu E.J., Puig O., Chaves F.J., Soutar A.K., Armengod M.E., Knecht E. A single point mutation in the low-density lipoprotein receptor switches the degradation of its mature protein from theproteasome to the lysosome // Int J Biochem Cell Biol. - 2006. - Vol.38(8). - P.1340-51.
2. Chen C.-H., Shaikenov T., Aimbetov R., Peterson T.R., Bissenbaev A.K., Lee S.-W., Wu J., Lin H.-K., Sarbassov D.D. ER stress inhibits mTORC2 and Akt signaling through GSK-3β-mediated phosphorylation of rictor // Science Signaling. - 2011. -Vol.4(161). - P.ra10.
3. Kannan N., Haste N., Taylor S.S., Neuwald A.F. The hallmark of AGC kinase functional divergence is its C-terminal tail, a cis-acting regulatory module // Proc Natl Acad Sci USA. - 2007. - Vol.104(4). - P.1272-7.
4. Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex // Science. - 2005. - Vol.307. - P.1098–1101.
5. Jones K.T., Greer E.R., Pearce D., Ashrafi K. Rictor/TORC2 regulates Caenorhabditis elegans fat storage, body size, and development through sgk-1 // PLoS Biol. - 2009. - Vol.7. - P.0604-0615.
6. Soukas A.A., Kane E.A., Carr C.E., Melo J.A., Ruvkun G. Rictor/TORC2 regulates fat metabolism, feeding, growth, and life span in Caenorhabditis elegans // Genes Dev. - 2009. - Vol.23. - P.496-511.
7. Sarbassov D.D., Ali S.M., Kim D.H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton // Curr Biol. - 2004. - Vol.14. - P.1296–1302.
8. Martín de Llano J.J., Fuertes G., Andreu E.J., Puig O., Chaves F.J., Soutar A.K., Armengod M.E., Knecht E. A single point mutation in the low-density lipoprotein receptor switches the degradation of its mature protein from theproteasome to the lysosome // Int J Biochem Cell Biol. - 2006. - Vol.38(8). - P.1340-51.
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How to Cite
Аимбетов, Р. С., Бисенбаев, А. К., & Сарбасов, Д. Д. (2017). GLY-934 ОБЕСПЕЧИВАЕТ ВЗАИМОДЕЙСТВИЕ РИКТОРА С SIN1. Experimental Biology, 56(4), 145–150. Retrieved from https://bb.kaznu.kz/index.php/biology/article/view/374
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BIOTECHNOLOGY
