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Translocation of TRAF proteins regulates apoptotic threshold of cells

R H Arch1, R W Gedrich, C B Thompson

  • 1Gwen Knapp Center for Lupus and Immunology Research, Howard Hughes Medical Institute, Department of Medicine, University of Chicago, IL 60637, USA. rarch@im.wustl.edu

Insights

Tumor necrosis factor (TNF) receptor-associated factors (TRAFs) redistribute within cells upon receptor activation. This TRAF2 translocation impacts cellular apoptosis sensitivity and signal transduction.

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Immunology

Background:

  • Tumor necrosis factor (TNF) receptor-associated factors (TRAFs) mediate signaling from TNF receptor (TNFR) family members.
  • TRAFs assemble into multiprotein complexes that regulate transcription factor nuclear factor kappaB (NF-kappaB) and c-Jun N-terminal kinase (JNK) activation.
  • The role of TRAF complex dynamics in apoptosis regulation remains unclear.

Purpose of the Study:

  • To investigate the intracellular fate of TRAF-containing complexes after receptor activation.
  • To determine how TRAF2 redistribution affects cellular responses to TNF-alpha.
  • To elucidate the mechanisms regulating TRAF-dependent signal transduction.

Main Methods:

  • Stimulation of TNFR family members and TRAF2 interaction with A20.
  • Analysis of TRAF2 intracellular localization and pool dynamics.
  • Assessment of cellular sensitivity to TNF-alpha-induced apoptosis.

Main Results:

  • Crosslinking of TNFRs or A20 interaction with TRAF2 induces TRAF2 translocation.
  • This redistribution depletes the cytoplasmic pool of TRAF2.
  • The ratio of soluble to insoluble TRAF2 correlates with TNF-alpha-induced apoptosis sensitivity.

Conclusions:

  • TRAF2 intracellular translocation is a key event following receptor activation.
  • TRAF2 pool dynamics regulate cellular apoptosis sensitivity.
  • TRAF redistribution may limit sustained TRAF-dependent signaling.

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