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10.1016/j.molcel.2015.03.034 http://scihub22266oqcxt.onion/10.1016/j.molcel.2015.03.034 C4458193!4458193!25936804     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25936804.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Mol+Cell 2015 ; 58 (5): 767-79 Nephropedia Template TP {{tp|p=25936804|t=2015. An Inhibitor of PIDDosome Formation |pdf=|usr=}}{{25936804}} gab.com Text An Inhibitor of PIDDosome Formation JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25936804 #FOAvip The PIDDosome?PIDD-RAIDD-caspase-2 complex?is a proapoptotic caspase-activation platform of elusive significance. DNA damage can initiate complex assembly via ATM phosphorylation of the PIDD death domain (DD), which enables RAIDD recruitment to PIDD. In contrast, the mechanisms limiting PIDDosome formation have remained unclear. We identify the mitotic checkpoint factor, BubR1, as a direct PIDDosome inhibitor, acting in a noncanonical role independent of Mad2. Following its phosphorylation by ATM at DNA breaks, ?primed? PIDD relocates to kinetochores via a direct interaction with BubR1. BubR1 binds the PIDD DD, competes with RAIDD recruitment, and negates PIDDosome-mediated apoptosis after ionizing radiation. The PIDDosome thus sequentially integrates DNA damage and mitotic checkpoint signals to decide cell fate in response to genotoxic stress. We further show that by sequestering PIDD at the kinetochore, BubR1 acts to delay PIDDosome formation until the next cycle, defining a new mechanism by which cells evade apoptosis during mitosis. Twit Text FOAVip An Inhibitor of PIDDosome Formation ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=25936804 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25936804 #FOAvip English Wikipedia <ref>{{Cite pmid|25936804}}</ref> An Inhibitor of PIDDosome Formation #MMPMID25936804 Thompson R; Shah RB; Liu PH; Gupta Y; Ando K; Aggarwal AK; Sidi S Mol Cell 2015[Jun]; 58 (5): 767-79 PMID25936804show ga The PIDDosome?PIDD-RAIDD-caspase-2 complex?is a proapoptotic caspase-activation platform of elusive significance. DNA damage can initiate complex assembly via ATM phosphorylation of the PIDD death domain (DD), which enables RAIDD recruitment to PIDD. In contrast, the mechanisms limiting PIDDosome formation have remained unclear. We identify the mitotic checkpoint factor, BubR1, as a direct PIDDosome inhibitor, acting in a noncanonical role independent of Mad2. Following its phosphorylation by ATM at DNA breaks, ?primed? PIDD relocates to kinetochores via a direct interaction with BubR1. BubR1 binds the PIDD DD, competes with RAIDD recruitment, and negates PIDDosome-mediated apoptosis after ionizing radiation. The PIDDosome thus sequentially integrates DNA damage and mitotic checkpoint signals to decide cell fate in response to genotoxic stress. We further show that by sequestering PIDD at the kinetochore, BubR1 acts to delay PIDDosome formation until the next cycle, defining a new mechanism by which cells evade apoptosis during mitosis. äAn Inhibitor of PIDDosome Formation (epmc).pdf DeepDyve Pubget Overpricing