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10.7554/eLife.19360 http://scihub22266oqcxt.onion/10.7554/eLife.19360 C5106211!5106211 !27787197     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\27787197 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Elife 2016 ; 5 (ä): ä Nephropedia Template TP {{tp|p=27787197 |t=2016. Regulation of mTORC1 by lysosomal calcium and calmodulin |pdf=|usr=}}{{27787197 }} gab.com Text Regulation of mTORC1 by lysosomal calcium and calmodulin JO: Elife http://www.kidney.de/pget.php?&tw=1&pmid=27787197 #FOAvip Blockade of lysosomal calcium release due to lysosomal lipid accumulation has been shown to inhibit mTORC1 signaling. However, the mechanism by which lysosomal calcium regulates mTORC1 has remained undefined. Herein we report that proper lysosomal calcium release through the calcium channel TRPML1 is required for mTORC1 activation. TRPML1 depletion inhibits mTORC1 activity, while overexpression or pharmacologic activation of TRPML1 has the opposite effect. Lysosomal calcium activates mTORC1 by inducing association of calmodulin (CaM) with mTOR. Blocking the interaction between mTOR and CaM by antagonists of CaM significantly inhibits mTORC1 activity. Moreover, CaM is capable of stimulating the kinase activity of mTORC1 in a calcium-dependent manner in vitro. These results reveal that mTOR is a new type of CaM-dependent kinase, and TRPML1, lysosomal calcium and CaM play essential regulatory roles in the mTORC1 signaling pathway. Twit Text FOAVip Regulation of mTORC1 by lysosomal calcium and calmodulin ????Elife http://www.kidney.de/pget.php?&tw=1&pmid=27787197 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27787197 #FOAvip English Wikipedia <ref>{{Cite pmid|27787197 }}</ref> Regulation of mTORC1 by lysosomal calcium and calmodulin #MMPMID27787197 Li RJ ; Xu J ; Fu C ; Zhang J ; Zheng YG ; Jia H ; Liu JO Elife 2016[Oct]; 5 (ä): ä PMID27787197 show ga Blockade of lysosomal calcium release due to lysosomal lipid accumulation has been shown to inhibit mTORC1 signaling. However, the mechanism by which lysosomal calcium regulates mTORC1 has remained undefined. Herein we report that proper lysosomal calcium release through the calcium channel TRPML1 is required for mTORC1 activation. TRPML1 depletion inhibits mTORC1 activity, while overexpression or pharmacologic activation of TRPML1 has the opposite effect. Lysosomal calcium activates mTORC1 by inducing association of calmodulin (CaM) with mTOR. Blocking the interaction between mTOR and CaM by antagonists of CaM significantly inhibits mTORC1 activity. Moreover, CaM is capable of stimulating the kinase activity of mTORC1 in a calcium-dependent manner in vitro. These results reveal that mTOR is a new type of CaM-dependent kinase, and TRPML1, lysosomal calcium and CaM play essential regulatory roles in the mTORC1 signaling pathway. |Calcium/*metabolism [MESH] |Calmodulin/*metabolism [MESH] |Cell Line [MESH] |Humans [MESH] |Lysosomes/*metabolism [MESH] |Mechanistic Target of Rapamycin Complex 1 [MESH] |Multiprotein Complexes/*metabolism [MESH] |Phosphorylation [MESH] |Protein Processing, Post-Translational [MESH] |Signal Transduction [MESH] |TOR Serine-Threonine Kinases/*metabolism [MESH]Regulation of mTORC1 by lysosomal calcium and calmodulin (epmc).pdf DeepDyve Pubget Overpricing