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10.7554/eLife.25158 http://scihub22266oqcxt.onion/10.7554/eLife.25158 C5391209!5391209!28406396     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       eLife 2017 ; 6 (ä): ä Nephropedia Template TP {{tp|p=28406396|t=2017. SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation |pdf=|usr=}}{{28406396}} gab.com Text SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation JO: eLife http://www.kidney.de/pget.php?&tw=1&pmid=28406396 #FOAvip The Ras family of GTPases are important in cell signaling and frequently mutated in human tumors. Understanding their regulation is thus important for studying biology and human diseases. Here, we report that a novel posttranslational mechanism, reversible lysine fatty acylation, regulates R-Ras2, a member of the Ras family. SIRT6, a sirtuin with established tumor suppressor function, regulates the lysine fatty acylation of R-Ras2. In mouse embryonic fibroblasts (MEFs), Sirt6 knockout (KO) increased R-Ras2 lysine fatty acylation. Lysine fatty acylation promotes the plasma membrane localization of R-Ras2 and its interaction with phosphatidylinositol 3-kinase PI3K, leading to activated Akt and increased cell proliferation. Our study establishes lysine fatty acylation as a previously unknown mechanism that regulates the Ras family of GTPases and provides an important mechanism by which SIRT6 functions as a tumor suppressor.DOI:http://dx.doi.org/10.7554/eLife.25158.001 Twit Text FOAVip SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation ????eLife http://www.kidney.de/pget.php?&tw=1&pmid=28406396 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28406396 #FOAvip English Wikipedia <ref>{{Cite pmid|28406396}}</ref> SIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation #MMPMID28406396 Zhang X; Spiegelman NA; Nelson OD; Jing H; Lin H eLife 2017[]; 6 (ä): ä PMID28406396show ga The Ras family of GTPases are important in cell signaling and frequently mutated in human tumors. Understanding their regulation is thus important for studying biology and human diseases. Here, we report that a novel posttranslational mechanism, reversible lysine fatty acylation, regulates R-Ras2, a member of the Ras family. SIRT6, a sirtuin with established tumor suppressor function, regulates the lysine fatty acylation of R-Ras2. In mouse embryonic fibroblasts (MEFs), Sirt6 knockout (KO) increased R-Ras2 lysine fatty acylation. Lysine fatty acylation promotes the plasma membrane localization of R-Ras2 and its interaction with phosphatidylinositol 3-kinase PI3K, leading to activated Akt and increased cell proliferation. Our study establishes lysine fatty acylation as a previously unknown mechanism that regulates the Ras family of GTPases and provides an important mechanism by which SIRT6 functions as a tumor suppressor.DOI:http://dx.doi.org/10.7554/eLife.25158.001 äSIRT6 regulates Ras-related protein R-Ras2 by lysine defatty-acylation(epmc).pdf DeepDyve Pubget Overpricing