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• W2061837661 abstract "Background The mammalian target of rapamycin (mTOR) belongs to the family of phosphoinositide (PI)-kinase-related kinases that includes the ataxia-telangiectasia gene product (ATM). mTOR plays a critical role in controlling translational effectors such as p70 S6 kinase α (p70α) and eukaryotic initiation factor 4E binding protein 1 (4EBP1). Results We show that the C-terminal region of mTOR, which is highly conserved among the PI-kinase-related kinases, plays a critical role in the mTOR protein kinase activity. Deletion of the C-terminal residues did not adversely affect the expression of mTOR, but caused a nearly complete loss of the mTOR protein kinase activity toward both 4EBP1 and p70αin vitro. These deletions also abolished the ability of a rapamycin-resistant mTOR mutant to rescue the activity of p70α from inhibition induced by rapamycin in vivo. Furthermore, replacement of Trp2545, a conserved residue in the C-terminal region throughout the PI-kinase-related kinase family, abolished the function of the mTOR kinase, both in vivo and in vitro. However, substitution of 32 C-terminal residues of mTOR with those of ATM did not restore the mTOR function. Conclusions These findings define an indispensable role for the noncatalytic C-terminal region of mTOR and indicate that, although this highly conserved region may be important throughout the PI-kinase-related kinase family, it is not functionally interchangeable within the family." @default.
• W2061837661 created "2016-06-24" @default.
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• W2061837661 date "2000-09-01" @default.
• W2061837661 modified "2023-09-25" @default.
• W2061837661 title "Carboxyl-terminal region conserved among phosphoinositide-kinase-related kinases is indispensable for mTOR functionin vivoandin vitro" @default.
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• W2061837661 doi "https://doi.org/10.1046/j.1365-2443.2000.00365.x" @default.
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