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10.1093/nar/gkw1202 http://scihub22266oqcxt.onion/10.1093/nar/gkw1202 C5389694!5389694!27923994     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       Nucleic+Acids+Res 2017 ; 45 (4): 1820-34 Nephropedia Template TP {{tp|p=27923994|t=2017. SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage |pdf=|usr=}}{{27923994}} gab.com Text SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=27923994 #FOAvip Telomere repeat binding factor 2 (TRF2) has been increasingly recognized to be involved in telomere maintenance and DNA damage response. Here, we show that TRF2 directly binds SIRT6 in a DNA independent manner and that this interaction is increased upon replication stress. Knockdown of SIRT6 up-regulates TRF2 protein levels and counteracts its down-regulation during DNA damage response, leading to cell survival. Moreover, we report that SIRT6 deactetylates in vivo the TRFH domain of TRF2, which in turn, is ubiquitylated in vivo activating the ubiquitin-dependent proteolysis. Notably, overexpression of the TRF2cT mutant failed to be stabilized by SIRT6 depletion, demonstrating that the TRFH domain is required for its post-transcriptional modification. Finally, we report an inverse correlation between SIRT6 and TRF2 protein expression levels in a cohort of colon rectal cancer patients. Taken together our findings describe TRF2 as a novel SIRT6 substrate and demonstrate that acetylation of TRF2 plays a crucial role in the regulation of TRF2 protein stability, thus providing a new route for modulating its expression level during oncogenesis and damage response. Twit Text FOAVip SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=27923994 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27923994 #FOAvip English Wikipedia <ref>{{Cite pmid|27923994}}</ref> SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage #MMPMID27923994 Rizzo A; Iachettini S; Salvati E; Zizza P; Maresca C; D'Angelo C; Benarroch-Popivker D; Capolupo A; del Gaudio F; Cosconati S; Di Maro S; Merlino F; Novellino E; Amoreo CA; Mottolese M; Sperduti I; Gilson E; Biroccio A Nucleic Acids Res 2017[Feb]; 45 (4): 1820-34 PMID27923994show ga Telomere repeat binding factor 2 (TRF2) has been increasingly recognized to be involved in telomere maintenance and DNA damage response. Here, we show that TRF2 directly binds SIRT6 in a DNA independent manner and that this interaction is increased upon replication stress. Knockdown of SIRT6 up-regulates TRF2 protein levels and counteracts its down-regulation during DNA damage response, leading to cell survival. Moreover, we report that SIRT6 deactetylates in vivo the TRFH domain of TRF2, which in turn, is ubiquitylated in vivo activating the ubiquitin-dependent proteolysis. Notably, overexpression of the TRF2cT mutant failed to be stabilized by SIRT6 depletion, demonstrating that the TRFH domain is required for its post-transcriptional modification. Finally, we report an inverse correlation between SIRT6 and TRF2 protein expression levels in a cohort of colon rectal cancer patients. Taken together our findings describe TRF2 as a novel SIRT6 substrate and demonstrate that acetylation of TRF2 plays a crucial role in the regulation of TRF2 protein stability, thus providing a new route for modulating its expression level during oncogenesis and damage response. äSIRT6 interacts with TRF2 and promotes its degradation in response to (epmc).pdf DeepDyve Pubget Overpricing