PMID- 9606216
OWN - NLM
STAT- MEDLINE
DCOM- 19980701
LR  - 20240213
IS  - 0021-9525 (Print)
IS  - 1540-8140 (Electronic)
IS  - 0021-9525 (Linking)
VI  - 141
IP  - 5
DP  - 1998 Jun 1
TI  - E1B 19K inhibits Fas-mediated apoptosis through FADD-dependent sequestration of 
      FLICE.
PG  - 1255-66
AB  - E1B 19K, the adenovirus Bcl-2 homologue, is a potent inhibitor of apoptosis 
      induced by various stimuli including Fas and tumor necrosis factor-alpha. Fas and 
      TNFR-1 belong to a family of cytokine-activated receptors that share key 
      components in their signaling pathways, Fas-associating protein with death domain 
      (FADD) and FADD-like interleukin-1beta-converting enzyme (FLICE), to induce an 
      apoptotic response. We demonstrate here that E1B 19K and Bcl-xL are able to 
      inhibit apoptosis induced by FADD, but not FLICE. Surprisingly, apoptosis was 
      abrogated by E1B 19K and Bcl-xL when FADD and FLICE were coexpressed. 
      Immunofluorescence studies demonstrated that FADD expression produced large 
      insoluble death effector filaments that may represent oligomerized FADD. E1B 19K 
      expression disrupted FADD filament formation causing FADD and FLICE to relocalize 
      to membrane and cytoskeletal structures where E1B 19K is normally localized. E1B 
      19K, however, does not detectably bind to FADD, nor does it inhibit FADD and 
      FLICE from being recruited to the death-inducing signaling complex (DISC) when 
      Fas is stimulated. Thus, E1B 19K may inhibit Fas-mediated cell death downstream 
      of FADD recruitment of FLICE but upstream of FLICE activation by disrupting FADD 
      oligomerization and sequestering an essential component of the DISC.
FAU - Perez, D
AU  - Perez D
AD  - Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, 
      New Jersey 08854, USA.
FAU - White, E
AU  - White E
LA  - eng
GR  - R01 CA053370/CA/NCI NIH HHS/United States
GR  - R37 CA053370/CA/NCI NIH HHS/United States
GR  - CA53370/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Adenovirus E1B Proteins)
RN  - 0 (BCL2L1 protein, human)
RN  - 0 (Carrier Proteins)
RN  - 0 (FADD protein, human)
RN  - 0 (Fas-Associated Death Domain Protein)
RN  - 0 (Proto-Oncogene Proteins c-bcl-2)
RN  - 0 (bcl-X Protein)
RN  - 0 (fas Receptor)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
RN  - EC 3.4.22.36 (Caspase 1)
SB  - IM
MH  - Actin Cytoskeleton/physiology
MH  - *Adaptor Proteins, Signal Transducing
MH  - Adenovirus E1B Proteins/*metabolism
MH  - *Apoptosis
MH  - Carrier Proteins/*metabolism
MH  - Caspase 1
MH  - Cysteine Endopeptidases/*metabolism
MH  - Enzyme Activation
MH  - Fas-Associated Death Domain Protein
MH  - HeLa Cells
MH  - Humans
MH  - Proto-Oncogene Proteins c-bcl-2/metabolism
MH  - bcl-X Protein
MH  - fas Receptor/*metabolism
PMC - PMC2137191
EDAT- 1998/06/12 00:00
MHDA- 1998/06/12 00:01
PMCR- 1998/12/01
CRDT- 1998/06/12 00:00
PHST- 1998/06/12 00:00 [pubmed]
PHST- 1998/06/12 00:01 [medline]
PHST- 1998/06/12 00:00 [entrez]
PHST- 1998/12/01 00:00 [pmc-release]
AID - 10.1083/jcb.141.5.1255 [doi]
PST - ppublish
SO  - J Cell Biol. 1998 Jun 1;141(5):1255-66. doi: 10.1083/jcb.141.5.1255.