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Casper/c-FLIP is physically and functionally associated with NF-kappa BI p105
Li, ZQ ; Zhang, JB ; Chen, DY ; Shu, HB
刊名生物化学与生物物理学研究通讯
2003
关键词Casper/c-FLIP p105 NF-kappa B caspase TUMOR-NECROSIS-FACTOR DOMAIN-CONTAINING PROTEIN CELL-DEATH INHIBITORY PROTEINS INDUCED APOPTOSIS CASPASE HOMOLOG KINASE COMPLEX C-FLIP ACTIVATION FADD
DOI10.1016/j.bbrc.2003.08.104
英文摘要Casper/c-FLIP is a caspase-8-related molecule critically involved in regulation of death receptor-induced apoptosis. It has been shown that Casper can either promote or antagonize apoptosis and can activate the transcription factor NF-kappaB. The exact functions of Casper are controversial. To further understand how Casper signals, we searched Casper-interacting proteins by yeast two-hybrid screening. This effort identified NF-kappaB1 (p105), an atypical IkappaB molecule and the precursor of NF-kappaB subunit p50. Co-immunoprecipitation experiments indicated that Casper interacted with p105 in 293 cells and this interaction was mediated through the C-terminal IkappaB-like domain (IkappaBgamma). Overexpression of p105 and IkappaBgamma inhibited Casper-induced NF-kappaB activation and potentiated Casper-induced apoptosis. Furthermore, Casper and its C-terminal caspase-like domain inhibited p105 processing into p50. Our findings suggest that p105 is involved in Casper-mediated regulation of apoptosis and NF-kappaB activation. (C) 2003 Elsevier Inc. All rights reserved.; Biochemistry & Molecular Biology; Biophysics; SCI(E); 0; ARTICLE; 4; 980-985; 309
语种英语
内容类型期刊论文
源URL[http://ir.pku.edu.cn/handle/20.500.11897/255642]  
专题生命科学学院
推荐引用方式
GB/T 7714
Li, ZQ,Zhang, JB,Chen, DY,et al. Casper/c-FLIP is physically and functionally associated with NF-kappa BI p105[J]. 生物化学与生物物理学研究通讯,2003.
APA Li, ZQ,Zhang, JB,Chen, DY,&Shu, HB.(2003).Casper/c-FLIP is physically and functionally associated with NF-kappa BI p105.生物化学与生物物理学研究通讯.
MLA Li, ZQ,et al."Casper/c-FLIP is physically and functionally associated with NF-kappa BI p105".生物化学与生物物理学研究通讯 (2003).
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