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Poly(ADP-ribosyl)ation regulates heat shock factor-1 activity and the heat shock response in murine fibroblasts

Silvia Fossati1, Laura Formentini, Zhao-Qi Wang

  • 1International Agency for Research on Cancer, Lyon, France.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|December 15, 2006
PubMed

Insights

Poly(ADP-ribose) polymerase-1 (PARP-1) activity regulates heat shock factor-1 (HSF-1) DNA binding and heat shock protein expression. PARP-1 deficiency enhances apoptosis and reduces survival signaling during heat shock.

Area of Science:

  • Molecular Biology
  • Cellular Stress Response

Background:

  • Poly(ADP-ribose) polymerase-1 (PARP-1) plays a role in transcriptional regulation.
  • The precise mechanisms and targets of PARP-1 in cellular responses are not fully understood.

Purpose of the Study:

  • To investigate the role of PARP-1 activity in the heat shock response of mouse fibroblasts.
  • To elucidate the molecular mechanisms by which PARP-1 influences heat shock factor-1 (HSF-1) and heat shock protein (HSP) expression.

Main Methods:

  • Assessed HSF-1 DNA binding in cellular extracts from PARP-1 wild-type and knockout mouse fibroblasts.
  • Quantified the expression of HSP-70 and HSP-27.
  • Evaluated JNK and NF-kappaB activation in response to heat shock.

Main Results:

  • PARP-1 activity impaired HSF-1 DNA binding.
  • HSF-1 DNA binding was higher in PARP-1 knockout cells.
  • Expression of HSP-70 and HSP-27 was enhanced in PARP-1 deficient cells.
  • PARP-1 null cells exhibited increased JNK activation and decreased NF-kappaB activity post-heat shock.

Conclusions:

  • Poly(ADP-ribosyl)ation by PARP-1 acts as a fine-tuner of HSF-1 activity.
  • PARP-1 has a complex, regulatory role in the mammalian cell's heat shock response, influencing both pro-apoptotic and prosurvival pathways.

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