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10.1158/2159-8290.CD-15-0460 http://scihub22266oqcxt.onion/10.1158/2159-8290.CD-15-0460 C4631654!4631654!26293922     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cancer+Discov 2015 ; 5 (11): 1194-209 Nephropedia Template TP {{tp|p=26293922|t=2015. PtdIns(3,4,5)P3-dependent Activation of the mTORC2 Kinase Complex |pdf=|usr=}}{{26293922}} gab.com Text PtdIns(3,4,5)P3-dependent Activation of the mTORC2 Kinase Complex JO: Cancer Discov http://www.kidney.de/pget.php?&tw=1&pmid=26293922 #FOAvip mTOR serves as a central regulator of cell growth and metabolism by forming two distinct complexes, mTORC1 and mTORC2. Although mechanisms of mTORC1 activation by growth factors and amino acids have been extensively studied, the upstream regulatory mechanisms leading to mTORC2 activation remain largely elusive. Here, we report that the PH domain of Sin1, an essential and unique component of mTORC2, interacts with the mTOR kinase domain to suppress mTOR activity. More importantly, PtdIns(3,4,5)P3, but not other PtdInsPn species, interacts with Sin1-PH to release its inhibition on the mTOR kinase domain, thereby triggering mTORC2 activation. Mutating critical Sin1 residues that mediate PtdIns(3,4,5)P3 interaction inactivates mTORC2, whereas mTORC2 activity is pathologically increased by patient-derived mutations in the Sin1-PH domain, promoting cell growth and tumor formation. Together, our study unravels a PI3K-dependent mechanism for mTORC2 activation, allowing mTORC2 to activate Akt in a manner that is regulated temporally and spatially by PtdIns(3,4,5)P3. Twit Text FOAVip PtdIns(3,4,5)P3-dependent Activation of the mTORC2 Kinase Complex ????Cancer Discov http://www.kidney.de/pget.php?&tw=1&pmid=26293922 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26293922 #FOAvip English Wikipedia <ref>{{Cite pmid|26293922}}</ref> PtdIns(3,4,5)P3-dependent Activation of the mTORC2 Kinase Complex #MMPMID26293922 Liu P; Gan W; Chin YR; Ogura K; Guo J; Zhang J; Wang B; Blenis J; Cantley LC; Toker A; Su B; Wei W Cancer Discov 2015[Nov]; 5 (11): 1194-209 PMID26293922show ga mTOR serves as a central regulator of cell growth and metabolism by forming two distinct complexes, mTORC1 and mTORC2. Although mechanisms of mTORC1 activation by growth factors and amino acids have been extensively studied, the upstream regulatory mechanisms leading to mTORC2 activation remain largely elusive. Here, we report that the PH domain of Sin1, an essential and unique component of mTORC2, interacts with the mTOR kinase domain to suppress mTOR activity. More importantly, PtdIns(3,4,5)P3, but not other PtdInsPn species, interacts with Sin1-PH to release its inhibition on the mTOR kinase domain, thereby triggering mTORC2 activation. Mutating critical Sin1 residues that mediate PtdIns(3,4,5)P3 interaction inactivates mTORC2, whereas mTORC2 activity is pathologically increased by patient-derived mutations in the Sin1-PH domain, promoting cell growth and tumor formation. Together, our study unravels a PI3K-dependent mechanism for mTORC2 activation, allowing mTORC2 to activate Akt in a manner that is regulated temporally and spatially by PtdIns(3,4,5)P3. äPtdIns(3,4,5)P3-dependent Activation of the mTORC2 Kinase Complex (epmc).pdf DeepDyve Pubget Overpricing