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10.15252/embj.201797072 http://scihub22266oqcxt.onion/10.15252/embj.201797072 C6043850!6043850!29875129     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2018 ; 37 (14): ä Nephropedia Template TP {{tp|p=29875129|t=2018. Dimer?specific immunoprecipitation of active caspase?2 identifies TRAF proteins as novel activators |pdf=|usr=}}{{29875129}} gab.com Text Dimer specific immunoprecipitation of active caspase 2 identifies TRAF proteins as novel activators JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=29875129 #FOAvip Caspase?2 has been shown to initiate apoptotic cell death in response to specific intracellular stressors such as DNA damage. However, the molecular mechanisms immediately upstream of its activation are still poorly understood. We combined a caspase?2 bimolecular fluorescence complementation (BiFC) system with fluorophore?specific immunoprecipitation to isolate and study the active caspase?2 dimer and its interactome. Using this technique, we found that tumor necrosis factor receptor?associated factor 2 (TRAF2), as well as TRAF1 and 3, directly binds to the active caspase?2 dimer. TRAF2 in particular is necessary for caspase?2 activation in response to apoptotic cell death stimuli. Furthermore, we found that dimerized caspase?2 is ubiquitylated in a TRAF2?dependent manner at K15, K152, and K153, which in turn stabilizes the active caspase?2 dimer complex, promotes its association with an insoluble cellular fraction, and enhances its activity to fully commit the cell to apoptosis. Together, these data indicate that TRAF2 positively regulates caspase?2 activation and consequent cell death by driving its activation through dimer?stabilizing ubiquitylation. Twit Text FOAVip Dimer specific immunoprecipitation of active caspase 2 identifies TRAF proteins as novel activators ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=29875129 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29875129 #FOAvip English Wikipedia <ref>{{Cite pmid|29875129}}</ref> Dimer?specific immunoprecipitation of active caspase?2 identifies TRAF proteins as novel activators #MMPMID29875129 Robeson AC; Lindblom KR; Wojton J; Kornbluth S; Matsuura K EMBO J 2018[Jul]; 37 (14): ä PMID29875129show ga Caspase?2 has been shown to initiate apoptotic cell death in response to specific intracellular stressors such as DNA damage. However, the molecular mechanisms immediately upstream of its activation are still poorly understood. We combined a caspase?2 bimolecular fluorescence complementation (BiFC) system with fluorophore?specific immunoprecipitation to isolate and study the active caspase?2 dimer and its interactome. Using this technique, we found that tumor necrosis factor receptor?associated factor 2 (TRAF2), as well as TRAF1 and 3, directly binds to the active caspase?2 dimer. TRAF2 in particular is necessary for caspase?2 activation in response to apoptotic cell death stimuli. Furthermore, we found that dimerized caspase?2 is ubiquitylated in a TRAF2?dependent manner at K15, K152, and K153, which in turn stabilizes the active caspase?2 dimer complex, promotes its association with an insoluble cellular fraction, and enhances its activity to fully commit the cell to apoptosis. Together, these data indicate that TRAF2 positively regulates caspase?2 activation and consequent cell death by driving its activation through dimer?stabilizing ubiquitylation. äDimer?specific immunoprecipitation of active caspase?2 identifies TRAF(epmc).pdf DeepDyve Pubget Overpricing