PMID- 24398693
OWN - NLM
STAT- MEDLINE
DCOM- 20140428
LR  - 20220311
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 289
IP  - 7
DP  - 2014 Feb 14
TI  - The C-terminal domain of the long form of cellular FLICE-inhibitory protein 
      (c-FLIPL) inhibits the interaction of the caspase 8 prodomain with the 
      receptor-interacting protein 1 (RIP1) death domain and regulates caspase 
      8-dependent nuclear factor kappaB (NF-kappaB) activation.
PG  - 3876-87
LID - 10.1074/jbc.M113.506485 [doi]
AB  - Caspase 8 plays an essential role in the regulation of apoptotic and 
      non-apoptotic signaling pathways. The long form of cellular FLICE-inhibitory 
      protein (c-FLIPL) has been shown previously to regulate caspase 8-dependent 
      nuclear factor kappaB (NF-kappaB) activation by receptor-interacting protein 1 (RIP1) and 
      TNF receptor-associated factor 2 (TRAF2). In this study, the molecular mechanism 
      by which c-FLIPL regulates caspase 8-dependent NF-kappaB activation was further 
      explored in the human embryonic kidney cell line HEK 293 and variant cells barely 
      expressing caspase 8. The caspase inhibitor 
      benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone greatly diminished caspase 
      8-dependent NF-kappaB activation induced by Fas ligand (FasL) when c-FLIPL, but not 
      its N-terminal fragment c-FLIP(p43), was expressed. The prodomain of caspase 8 
      was found to interact with the RIP1 death domain and to be sufficient to mediate 
      NF-kappaB activation induced by FasL or c-FLIP(p43). The interaction of the RIP1 
      death domain with caspase 8 was inhibited by c-FLIPL but not c-FLIP(p43). Thus, 
      these results reveal that the C-terminal domain of c-FLIPL specifically inhibits 
      the interaction of the caspase 8 prodomain with the RIP1 death domain and, 
      thereby, regulates caspase 8-dependent NF-kappaB activation.
FAU - Matsuda, Iyo
AU  - Matsuda I
AD  - From the Department of Applied Biology, Kyoto Institute of Technology, 
      Matsugasaki, Sakyo-ku, Kyoto 606-8585, Japan and.
FAU - Matsuo, Kentaro
AU  - Matsuo K
FAU - Matsushita, Yuka
AU  - Matsushita Y
FAU - Haruna, Yasushi
AU  - Haruna Y
FAU - Niwa, Masamitsu
AU  - Niwa M
FAU - Kataoka, Takao
AU  - Kataoka T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140106
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (AGFG1 protein, human)
RN  - 0 (CASP8 and FADD-Like Apoptosis Regulating Protein)
RN  - 0 (CFLAR protein, human)
RN  - 0 (NF-kappa B)
RN  - 0 (Nuclear Pore Complex Proteins)
RN  - 0 (Protease Inhibitors)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (TNF Receptor-Associated Factor 2)
RN  - EC 3.4.22.- (CASP8 protein, human)
RN  - EC 3.4.22.- (Caspase 8)
SB  - IM
MH  - CASP8 and FADD-Like Apoptosis Regulating Protein/genetics/*metabolism
MH  - Caspase 8/genetics/*metabolism
MH  - HEK293 Cells
MH  - Humans
MH  - NF-kappa B/genetics/*metabolism
MH  - Nuclear Pore Complex Proteins/genetics/*metabolism
MH  - Protease Inhibitors/pharmacology
MH  - Protein Structure, Tertiary
MH  - RNA-Binding Proteins/genetics/*metabolism
MH  - TNF Receptor-Associated Factor 2/genetics/metabolism
MH  - U937 Cells
PMC - PMC3924257
OTO - NOTNLM
OT  - Caspase
OT  - Death Domain
OT  - Fas
OT  - NF-kappaB
OT  - RIP
EDAT- 2014/01/09 06:00
MHDA- 2014/04/29 06:00
PMCR- 2015/02/14
CRDT- 2014/01/09 06:00
PHST- 2014/01/09 06:00 [entrez]
PHST- 2014/01/09 06:00 [pubmed]
PHST- 2014/04/29 06:00 [medline]
PHST- 2015/02/14 00:00 [pmc-release]
AID - S0021-9258(20)44176-6 [pii]
AID - M113.506485 [pii]
AID - 10.1074/jbc.M113.506485 [doi]
PST - ppublish
SO  - J Biol Chem. 2014 Feb 14;289(7):3876-87. doi: 10.1074/jbc.M113.506485. Epub 2014 
      Jan 6.