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HSP70 interacts with TRAF2 and differentially regulates TNFalpha signalling in human colon cancer cells

Shengming Dai1, Lijun Jiang, Guisheng Wang

  • 1Department of Lab Science, The Fourth Hospital Affiliated to Guangxi Medical University, Liuzhou, China. shengming_dai@yahoo.com

Journal of Cellular and Molecular Medicine
|February 27, 2009
PubMed

Insights

Heat shock protein 70 (HSP70) differentially regulates tumor necrosis factor-alpha (TNFα) signaling in colon cancer. HSP70 inhibits NF-κB activation while promoting JNK activation via TRAF2 interaction, contributing to apoptosis.

Area of Science:

  • Cellular biology
  • Molecular oncology
  • Signal transduction

Background:

  • Tumor necrosis factor (TNF) family members induce survival and apoptosis.
  • Heat shock proteins (HSPs) protect cells from stress.
  • Mechanisms of HSPs in TNFα signaling remain unclear.

Purpose of the Study:

  • Investigate HSP70's role in TNFα-induced signaling pathways.
  • Elucidate HSP70's interaction with TNF receptor-associated factor 2 (TRAF2).
  • Determine HSP70's effect on NF-κB and JNK activation.

Main Methods:

  • Overexpression of HSP70 in human colon cancer cells.
  • Analysis of NF-κB and JNK activation.
  • Investigation of TRAF2 interactions and cellular localization.

Main Results:

  • HSP70 overexpression inhibited TNFα-induced NF-κB activation.
  • HSP70 promoted TNFα-induced JNK activation.
  • HSP70-TRAF2 interaction reduced NF-κB signaling complex recruitment.
  • HSP70-TRAF2 interaction enhanced JNK activation.

Conclusions:

  • HSP70 differentially regulates TNFα-induced NF-κB and JNK activation via TRAF2.
  • HSP70 contributes to TNFα-induced apoptosis in colon cancer cells.

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