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Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human

Y Zhan1, R Hegde, S M Srinivasula

  • 1Center for Apoptosis Research, Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, PA 19107, USA.

Cell Death and Differentiation
|April 20, 2002
PubMed

Insights

Researchers discovered FLAME-3, a novel nuclear protein. FLAME-3 interacts with transcription factor TFIIIC102, potentially regulating gene transcription and NF-kappaB promoter activity.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • Death effector domain (DED)-containing proteins regulate key cellular processes like apoptosis and transcription factor activation.
  • FLAME-3 is a newly identified nuclear DED-containing protein with homology to DEDD.

Purpose of the Study:

  • To identify and characterize the novel nuclear DED-containing protein FLAME-3.
  • To investigate the interactions of FLAME-3 with other DED proteins and its role in nuclear processes.

Main Methods:

  • Yeast two-hybrid system to identify protein interactions.
  • Overexpression studies in human cell lines (MCF-7, 293).
  • Luciferase reporter gene assay to assess promoter activity.

Main Results:

  • FLAME-3 interacts with DEDD and c-FLIP, but not FADD, caspase-8, or caspase-10.
  • FLAME-3, along with DEDD, interacts with and sequesters the TFIIIC102 subunit of human transcription factor TFIIIC in the nucleus.
  • Overexpression of FLAME-3 or DEDD inhibits NF-kappaB promoter-driven gene expression.

Conclusions:

  • FLAME-3 is a novel nuclear DED-containing protein involved in protein-protein interactions.
  • FLAME-3 and DEDD may regulate the activity of the human transcription factor TFIIIC complex.
  • This study provides evidence for DED-containing proteins in the nuclear regulation of general transcription machinery.

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