1. Cell Biology
  2. Computational and Systems Biology
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Heat Shock Response: A model for handling cell stress

  1. Laura Le Breton
  2. Matthias P Mayer  Is a corresponding author
  1. DKFZ-ZMBH-Alliance, Germany
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Cite this article as: eLife 2016;5:e22850 doi: 10.7554/eLife.22850
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Figures

The chaperone titration model of the heat shock response.

Clockwise from top: The chaperone protein Hsp70 binds to the heat shock transcription factor Hsf1, repressing its transcriptional activity. Upon a sudden increase in temperature or other stresses (red lightning bolt), fewer proteins maintain their correct shape (rectangles); misfolded proteins (stars) therefore accumulate in the cell. These misfolded proteins draw Hsp70 away from Hsf1, activating its transcriptional activity. As a result, more Hsf1-dependent genes (HDG) are expressed, leading to an increase in the number of chaperones and proteases – among them Hsp70 – in the cell. The action of the chaperones and proteases ensures that proteins can be correctly folded again; this also liberates Hsp70, which can then repress Hsf1. Middle: Hyperphosphorylation of Hsf1 (the width of the triangle represents the extent of phosphorylation) partially activates Hsf1 and sensitizes the regulatory feedback circuit.

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