PMID- 10187770
OWN - NLM
STAT- MEDLINE
DCOM- 19990503
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 15
DP  - 1999 Apr 9
TI  - CIPER, a novel NF kappaB-activating protein containing a caspase recruitment
      domain with homology to Herpesvirus-2 protein E10.
PG  - 9955-61
AB  - We have identified and characterized CIPER, a novel protein containing a caspase 
      recruitment domain (CARD) in its N terminus and a C-terminal region rich in
      serine and threonine residues. The CARD of CIPER showed striking similarity to
      E10, a product of the equine herpesvirus-2. CIPER formed homodimers via its CARD 
      and interacted with viral E10 but not with several apoptosis regulators
      containing CARDs including ARC, RAIDD, RICK, caspase-2, caspase-9, or Apaf-1.
      Expression of CIPER induced NF-kappaB activation, which was inhibited by
      dominant-negative NIK and a nonphosphorylable IkappaB-alpha mutant but not by
      dominant-negative RIP. Mutational analysis revealed that the N-terminal region of
      CIPER containing the CARD was sufficient and necessary for NF-kappaB-inducing
      activity. Point mutations in highly conserved residues in the CARD of CIPER
      disrupted the ability of CIPER to activate NF-kappaB and to form homodimers,
      indicating that the CARD is essential for NF-kappaB activation and dimerization. 
      We propose that CIPER acts in a NIK-dependent pathway of NF-kappaB activation.
FAU - Koseki, T
AU  - Koseki T
AD  - Department of Pathology and Comprehensive Cancer Center, The University of
      Michigan Medical School, Ann Arbor, Michigan 48109, USA.
FAU - Inohara, N
AU  - Inohara N
FAU - Chen, S
AU  - Chen S
FAU - Carrio, R
AU  - Carrio R
FAU - Merino, J
AU  - Merino J
FAU - Hottiger, M O
AU  - Hottiger MO
FAU - Nabel, G J
AU  - Nabel GJ
FAU - Nunez, G
AU  - Nunez G
LA  - eng
SI  - GENBANK/AF057700
SI  - GENBANK/AF057701
GR  - CA-64421/CA/NCI NIH HHS/United States
GR  - CA-64556/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (APAF1 protein, human)
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Apaf1 protein, mouse)
RN  - 0 (Apoptotic Protease-Activating Factor 1)
RN  - 0 (B-Cell CLL-Lymphoma 10 Protein)
RN  - 0 (BCL10 protein, human)
RN  - 0 (Bcl10 protein, mouse)
RN  - 0 (Caenorhabditis elegans Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (NF-kappa B)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteins)
RN  - EC 3.4.22.- (CASP9 protein, human)
RN  - EC 3.4.22.- (Casp9 protein, mouse)
RN  - EC 3.4.22.- (Caspase 2)
RN  - EC 3.4.22.- (Caspase 9)
RN  - EC 3.4.22.- (Caspases)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
RN  - EC 3.4.22.- (ced-3 protein, C elegans)
SB  - IM
MH  - *Adaptor Proteins, Signal Transducing
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Apoptosis
MH  - Apoptotic Protease-Activating Factor 1
MH  - B-Cell CLL-Lymphoma 10 Protein
MH  - Blotting, Northern
MH  - Caenorhabditis elegans Proteins
MH  - Carrier Proteins/chemistry/metabolism
MH  - Caspase 2
MH  - Caspase 9
MH  - Caspases/chemistry/*metabolism
MH  - Cysteine Endopeptidases/chemistry
MH  - Enzyme Activation
MH  - Expressed Sequence Tags
MH  - Humans
MH  - Jurkat Cells
MH  - Mice
MH  - Molecular Sequence Data
MH  - NF-kappa B/*metabolism
MH  - Neoplasm Proteins/chemistry/*genetics/physiology
MH  - Point Mutation
MH  - Proteins/chemistry
MH  - *Sequence Homology, Amino Acid
EDAT- 1999/04/03 00:00
MHDA- 1999/04/03 00:01
CRDT- 1999/04/03 00:00
PHST- 1999/04/03 00:00 [pubmed]
PHST- 1999/04/03 00:01 [medline]
PHST- 1999/04/03 00:00 [entrez]
AID - 10.1074/jbc.274.15.9955 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 9;274(15):9955-61. doi: 10.1074/jbc.274.15.9955.