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10.1158/0008-5472.CAN-15-2498 http://scihub22266oqcxt.onion/10.1158/0008-5472.CAN-15-2498 C4930699!4930699!27197174     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cancer+Res 2016 ; 76 (13): 3802-12 Nephropedia Template TP {{tp|p=27197174|t=2016. SIRT2-mediated deacetylation and tetramerization of pyruvate kinase directs glycolysis and tumor growth |pdf=|usr=}}{{27197174}} gab.com Text SIRT2-mediated deacetylation and tetramerization of pyruvate kinase directs glycolysis and tumor growth JO: Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=27197174 #FOAvip Sirtuins participate in sensing nutrient availability and directing metabolic activity to match energy needs with energy production and consumption. However, the pivotal targets for sirtuins in cancer are mainly unknown. In this study, we identify the M2 isoform of pyruvate kinase (PKM2) as a critical target of the sirtuin SIRT2 implicated in cancer. PKM2 directs the synthesis of pyruvate and acetyl-CoA, the latter of which is transported to mitochondria for use in the Krebs cycle to generate ATP. Enabled by a shotgun mass spectrometry analysis founded on tissue culture models, we identified a candidate SIRT2 deacetylation target at PKM2 lysine 305 (K305). Biochemical experiments including site-direct mutants that mimicked constitutive acetylation suggested that acetylation reduced PKM2 activity by preventing tetramerization to the active enzymatic form. Notably, ectopic overexpression of a deacetylated PKM2 mutant in Sirt2-deficient mammary tumor cells altered glucose metabolism and inhibited malignant growth. Taken together, our results argued that loss of SIRT2 function in cancer cells reprograms their glycolytic metabolism via PKM2 regulation, partially explaining the tumor-permissive phenotype of mice lacking Sirt2. Twit Text FOAVip SIRT2-mediated deacetylation and tetramerization of pyruvate kinase directs glycolysis and tumor growth ????Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=27197174 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27197174 #FOAvip English Wikipedia <ref>{{Cite pmid|27197174}}</ref> SIRT2-mediated deacetylation and tetramerization of pyruvate kinase directs glycolysis and tumor growth #MMPMID27197174 Park SH; Ozden O; Liu G; Song HY; Zhu Y; Yan Y; Zou X; Kang HJ; Jiang H; Principe DR; Cha YI; Roh M; Vassilopoulos A; Gius D Cancer Res 2016[Jul]; 76 (13): 3802-12 PMID27197174show ga Sirtuins participate in sensing nutrient availability and directing metabolic activity to match energy needs with energy production and consumption. However, the pivotal targets for sirtuins in cancer are mainly unknown. In this study, we identify the M2 isoform of pyruvate kinase (PKM2) as a critical target of the sirtuin SIRT2 implicated in cancer. PKM2 directs the synthesis of pyruvate and acetyl-CoA, the latter of which is transported to mitochondria for use in the Krebs cycle to generate ATP. Enabled by a shotgun mass spectrometry analysis founded on tissue culture models, we identified a candidate SIRT2 deacetylation target at PKM2 lysine 305 (K305). Biochemical experiments including site-direct mutants that mimicked constitutive acetylation suggested that acetylation reduced PKM2 activity by preventing tetramerization to the active enzymatic form. Notably, ectopic overexpression of a deacetylated PKM2 mutant in Sirt2-deficient mammary tumor cells altered glucose metabolism and inhibited malignant growth. Taken together, our results argued that loss of SIRT2 function in cancer cells reprograms their glycolytic metabolism via PKM2 regulation, partially explaining the tumor-permissive phenotype of mice lacking Sirt2. äSIRT2-mediated deacetylation and tetramerization of pyruvate kinase di(epmc).pdf DeepDyve Pubget Overpricing