PMID- 10544233
OWN - NLM
STAT- MEDLINE
DCOM- 19991210
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 460
IP  - 2
DP  - 1999 Oct 29
TI  - Functional interaction of Fas-associated phosphatase-1 (FAP-1) with p75(NTR) and 
      their effect on NF-kappaB activation.
PG  - 191-8
AB  - The common neurotrophin receptor p75(NTR), a member of the tumor necrosis factor 
      (TNF) receptor superfamily, plays an important role in several cellular signaling
      cascades, including that leading to apoptosis. FAP-1 (Fas-associated
      phosphatase-1), which binds to the cytoplasmic tail of Fas, was originally
      identified as a negative regulator of Fas-mediated apoptosis. Here we have shown 
      by co-immunoprecipitation that FAP-1 also binds to the p75(NTR) cytoplasmic
      domain in vivo through the interaction between the third PDZ domain of FAP-1 and 
      C-terminal Ser-Pro-Val residues of p75(NTR). Furthermore, cells expressing a
      FAP-1/green fluorescent protein showed intracellular co-localization of FAP-1 and
      p75(NTR) at the plasma membrane. To elucidate the functional role of this
      physical interaction, we examined TRAF6 (TNF receptor-associated factor
      6)-mediated NF-kappaB activation and tamoxifen-induced apoptosis in 293T cells
      expressing p75(NTR). The results revealed that TRAF6-mediated NF-kappaB
      activation was suppressed by p75(NTR) and that the p75(NTR)-mediated NF-kappaB
      suppression was reduced by FAP-1 expression. Interestingly, a mutant of the
      p75(NTR) intracellular domain with a single substitution of a Met for Val in its 
      C-terminus, which cannot interact with FAP-1, displayed enhanced pro-apoptotic
      activity in 293T transfected cells. Thus, similar to Fas, FAP-1 may be involved
      in suppressing p75(NTR)-mediated pro-apoptotic signaling through its interaction 
      with three C-terminal amino acids (tSPV). Thus, FAP-1 may regulate
      p75(NTR)-mediated signal transduction by physiological interaction through its
      third PDZ domain.
FAU - Irie, S
AU  - Irie S
AD  - Molecular Oncology Laboratory, Tsukuba Life Science Center, Institute of Physical
      and Chemical Research (RIKEN), Ibaraki, Japan. irie@rtc.riken.go.jp
FAU - Hachiya, T
AU  - Hachiya T
FAU - Rabizadeh, S
AU  - Rabizadeh S
FAU - Maruyama, W
AU  - Maruyama W
FAU - Mukai, J
AU  - Mukai J
FAU - Li, Y
AU  - Li Y
FAU - Reed, J C
AU  - Reed JC
FAU - Bredesen, D E
AU  - Bredesen DE
FAU - Sato, T A
AU  - Sato TA
LA  - eng
SI  - GENBANK/AF233323
GR  - R01 GM055147/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Carrier Proteins)
RN  - 0 (NF-kappa B)
RN  - 0 (Proteins)
RN  - 0 (Receptor, Nerve Growth Factor)
RN  - 0 (TNF Receptor-Associated Factor 6)
RN  - EC 1.13.12.- (Luciferases)
RN  - EC 2.5.1.18 (Glutathione Transferase)
RN  - EC 3.1.3.16 (Protein Phosphatase 1)
RN  - EC 3.1.3.48 (PTPN13 protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 13)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
SB  - IM
MH  - Carrier Proteins/*metabolism
MH  - Cell Line
MH  - Down-Regulation
MH  - Glutathione Transferase/metabolism
MH  - Humans
MH  - Luciferases/metabolism
MH  - Mutagenesis
MH  - NF-kappa B/*metabolism
MH  - Plasmids
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Phosphatase 1
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 13
MH  - Protein Tyrosine Phosphatases/*metabolism
MH  - Proteins/metabolism
MH  - Receptor, Nerve Growth Factor/*metabolism
MH  - Signal Transduction
MH  - TNF Receptor-Associated Factor 6
MH  - Transfection
MH  - Up-Regulation
EDAT- 1999/11/02 00:00
MHDA- 1999/11/02 00:01
CRDT- 1999/11/02 00:00
PHST- 1999/11/02 00:00 [pubmed]
PHST- 1999/11/02 00:01 [medline]
PHST- 1999/11/02 00:00 [entrez]
AID - S0014-5793(99)01324-1 [pii]
AID - 10.1016/s0014-5793(99)01324-1 [doi]
PST - ppublish
SO  - FEBS Lett. 1999 Oct 29;460(2):191-8. doi: 10.1016/s0014-5793(99)01324-1.