PMID- 9647239
OWN - NLM
STAT- MEDLINE
DCOM- 19980709
LR  - 20100825
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 161
IP  - 1
DP  - 1998 Jul 1
TI  - The N-terminal domains target TNF receptor-associated factor-2 to the nucleus and 
      display transcriptional regulatory activity.
PG  - 319-24
AB  - The subcellular localization of the TNF receptor-associated factor-2 (TRAF2) 
      adaptor protein in human endothelial cells, which mediates proinflammatory 
      responses of TNF, has been analyzed by confocal immunofluorescence microscopy and 
      by Western blotting of fractionated cell extracts. Rabbit antisera reactive with 
      either amino- or carboxyl-terminal TRAF2 peptides frequently but not uniformly 
      stain nuclei of cultured HUVEC or the established human endothelial cell line, 
      ECV304. However, Western blotting reveals significant heterogeneity in the 
      reactivities of these polyclonal Abs. Transiently transfected HUVEC expressing 
      FLAG epitope-tagged TRAF2 consistently show prominent nuclear localization, and 
      deletion mutants of TRAF2 identify the portion of the molecule responsible for 
      nuclear localization as the amino-terminal ring finger domain. TNF treatment does 
      not appear to influence the localization of endogenous or transfected TRAF2 
      protein. Transfection of the amino-terminal half of the TRAF2 molecule, 
      containing the ring and zinc finger domains, which localizes to the nucleus, 
      results in activation of E-selectin but not of NF-kappaB promoter-reporter gene 
      transcription or of c-Jun N-terminal kinase activation. These observations 
      suggest that TRAF2 may reside in the nucleus and directly regulate transcription, 
      independent of its role in cytoplasmic signal transduction.
FAU - Min, W
AU  - Min W
AD  - Boyer Center for Molecular Medicine, Yale University School of Medicine, New 
      Haven, CT 06536, USA.
FAU - Bradley, J R
AU  - Bradley JR
FAU - Galbraith, J J
AU  - Galbraith JJ
FAU - Jones, S J
AU  - Jones SJ
FAU - Ledgerwood, E C
AU  - Ledgerwood EC
FAU - Pober, J S
AU  - Pober JS
LA  - eng
GR  - HL-36003/HL/NHLBI NIH HHS/United States
GR  - T32-AI07019/AI/NIAID NIH HHS/United States
GR  - Wellcome Trust/United Kingdom
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 Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteins)
RN  - 0 (Receptors, Tumor Necrosis Factor)
RN  - 0 (TNF Receptor-Associated Factor 2)
SB  - IM
MH  - Biological Transport/genetics/immunology
MH  - Cell Nucleus/genetics/*metabolism
MH  - Cells, Cultured
MH  - Cytoplasm/immunology/metabolism
MH  - Endothelium, Vascular/cytology/metabolism
MH  - Fluorescent Antibody Technique, Indirect
MH  - Humans
MH  - Peptide Fragments/genetics/physiology
MH  - Protein Biosynthesis
MH  - Protein Structure, Tertiary
MH  - Proteins/genetics/*metabolism
MH  - Receptors, Tumor Necrosis Factor/*metabolism
MH  - TNF Receptor-Associated Factor 2
MH  - Transcription, Genetic/*immunology
MH  - Transfection/immunology
MH  - Umbilical Veins
EDAT- 1998/07/01 00:00
MHDA- 1998/07/01 00:01
CRDT- 1998/07/01 00:00
PHST- 1998/07/01 00:00 [pubmed]
PHST- 1998/07/01 00:01 [medline]
PHST- 1998/07/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1998 Jul 1;161(1):319-24.