Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.18632/oncotarget.8383 http://scihub22266oqcxt.onion/10.18632/oncotarget.8383 C5008269!5008269 !27027448     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27027448 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Oncotarget 2016 ; 7 (16 ): 21064-75 Nephropedia Template TP {{tp|p=27027448 |t=2016. PI3K/Akt promotes feedforward mTORC2 activation through IKK? |pdf=|usr=}}{{27027448 }} gab.com Text PI3K/Akt promotes feedforward mTORC2 activation through IKK JO: Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=27027448 #FOAvip The ser-thr Akt plays a critical role in the regulation of cell survival, cell growth and proliferation, as well as energy metabolism and is dysregulated in many cancers. The regulation of Akt activity depends on the phosphorylation at two sites: (i) Thr308 in the activation loop by phosphoinositide-dependent kinase-1 (PDK1) and (ii) Ser473 hydrophobic motif at the carboxyl terminus by a second activity termed PDK2, which is the mTORC2 complex composed of mTOR, rictor, and Sin1. Previously we demonstrated that IKK?, a component of the IKK complex that controls NF-?B activation, participates in the Akt-dependent regulation of mTORC1. Here we have explored a potential involvement of IKK? in controlling Akt activity and whether this may involve mTORC2. The experiments show that IKK? associates with mTORC2 in several cancer cells in a manner dependent on PI3K/Akt activity and that IKK? positively promotes Akt phosphorylation at Ser473 and at Thr308. Moreover, IKK? enhances mTORC2 kinase activity directed to Akt on Ser473 and Akt-mediated phosphorylation of FOXO3a and GSK3?, but not other Akt-associated targets such as TSC2 and PRAS40, indicating the existence of multiple mechanisms of Akt activation in cells. In addition, loss of IKK? suppresses growth factor-induced Akt activation associated with mTORC1 inhibition. These results indicate that IKK? serves as a feedforward regulator of mTORC2 and that IKK? could serve as a key therapeutic target to block mTORC2 and Akt activation in some cancers. Twit Text FOAVip PI3K/Akt promotes feedforward mTORC2 activation through IKK ????Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=27027448 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27027448 #FOAvip English Wikipedia <ref>{{Cite pmid|27027448 }}</ref> PI3K/Akt promotes feedforward mTORC2 activation through IKK? #MMPMID27027448 Dan HC ; Antonia RJ ; Baldwin AS Oncotarget 2016[Apr]; 7 (16 ): 21064-75 PMID27027448 show ga The ser-thr Akt plays a critical role in the regulation of cell survival, cell growth and proliferation, as well as energy metabolism and is dysregulated in many cancers. The regulation of Akt activity depends on the phosphorylation at two sites: (i) Thr308 in the activation loop by phosphoinositide-dependent kinase-1 (PDK1) and (ii) Ser473 hydrophobic motif at the carboxyl terminus by a second activity termed PDK2, which is the mTORC2 complex composed of mTOR, rictor, and Sin1. Previously we demonstrated that IKK?, a component of the IKK complex that controls NF-?B activation, participates in the Akt-dependent regulation of mTORC1. Here we have explored a potential involvement of IKK? in controlling Akt activity and whether this may involve mTORC2. The experiments show that IKK? associates with mTORC2 in several cancer cells in a manner dependent on PI3K/Akt activity and that IKK? positively promotes Akt phosphorylation at Ser473 and at Thr308. Moreover, IKK? enhances mTORC2 kinase activity directed to Akt on Ser473 and Akt-mediated phosphorylation of FOXO3a and GSK3?, but not other Akt-associated targets such as TSC2 and PRAS40, indicating the existence of multiple mechanisms of Akt activation in cells. In addition, loss of IKK? suppresses growth factor-induced Akt activation associated with mTORC1 inhibition. These results indicate that IKK? serves as a feedforward regulator of mTORC2 and that IKK? could serve as a key therapeutic target to block mTORC2 and Akt activation in some cancers. |*Gene Expression Regulation, Neoplastic [MESH] |Apoptosis [MESH] |Biomarkers, Tumor/*metabolism [MESH] |Cell Proliferation [MESH] |Humans [MESH] |I-kappa B Kinase/*metabolism [MESH] |Mechanistic Target of Rapamycin Complex 2/*metabolism [MESH] |Neoplasms/*metabolism/pathology [MESH] |Phosphatidylinositol 3-Kinases/*metabolism [MESH] |Phosphorylation [MESH] |Protein Binding [MESH] |Proto-Oncogene Proteins c-akt/*metabolism [MESH] |Signal Transduction [MESH]PI3K/Akt promotes feedforward mTORC2 activation through IKK? (epmc).pdf DeepDyve Pubget Overpricing