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10.1016/j.cell.2016.02.026 http://scihub22266oqcxt.onion/10.1016/j.cell.2016.02.026 C5018360!5018360!26949185     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2016 ; 165 (2): 421-33 Nephropedia Template TP {{tp|p=26949185|t=2016. BOK Is a Non-Canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation |pdf=|usr=}}{{26949185}} gab.com Text BOK Is a Non-Canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=26949185 #FOAvip The mitochondrial pathway of apoptosis is initiated by mitochondrial outer membrane permeabilization (MOMP). The BCL-2 family effectors BAX and BAK are thought to be absolute required for this process. Here we report that BCL-2 ovarian killer (BOK) is a bona fide yet unconventional effector of MOMP that can trigger apoptosis in the absence of both BAX and BAK. However, unlike the canonical effectors, BOK appears to be constitutively active and unresponsive to antagonistic effects of the antiapoptotic BCL-2 proteins. Rather, BOK is controlled at the level of protein stability by components of the endoplasmic reticulum?associated degradation pathway. BOK is ubiquitylated by the AMFR/gp78 E3 ubiquitin ligase complex and targeted for proteasomal degradation in a VCP/p97-dependent manner, which allows survival of the cell. When proteasome function, VCP, or gp78 activity is compromised, BOK is stabilized to induce MOMP and apoptosis independently of other BCL-2 proteins. Twit Text FOAVip BOK Is a Non-Canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=26949185 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26949185 #FOAvip English Wikipedia <ref>{{Cite pmid|26949185}}</ref> BOK Is a Non-Canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation #MMPMID26949185 Llambi F; Wang YM; Victor B; Yang M; Schneider DM; Gingras S; Parsons MJ; Zheng JH; Brown SA; Pelletier S; Moldoveanu T; Chen T; Green DR Cell 2016[Apr]; 165 (2): 421-33 PMID26949185show ga The mitochondrial pathway of apoptosis is initiated by mitochondrial outer membrane permeabilization (MOMP). The BCL-2 family effectors BAX and BAK are thought to be absolute required for this process. Here we report that BCL-2 ovarian killer (BOK) is a bona fide yet unconventional effector of MOMP that can trigger apoptosis in the absence of both BAX and BAK. However, unlike the canonical effectors, BOK appears to be constitutively active and unresponsive to antagonistic effects of the antiapoptotic BCL-2 proteins. Rather, BOK is controlled at the level of protein stability by components of the endoplasmic reticulum?associated degradation pathway. BOK is ubiquitylated by the AMFR/gp78 E3 ubiquitin ligase complex and targeted for proteasomal degradation in a VCP/p97-dependent manner, which allows survival of the cell. When proteasome function, VCP, or gp78 activity is compromised, BOK is stabilized to induce MOMP and apoptosis independently of other BCL-2 proteins. äBOK Is a Non-Canonical BCL-2 Family Effector of Apoptosis Regulated by(epmc).pdf DeepDyve Pubget Overpricing