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Heat shock protein 70 (Hsp70) phosphorylation at T495 occurs endogenously during DNA damage. This conserved modification regulates cell cycle progression and delays cell division, revealing fundamental cell biology insights.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Heat shock protein 70 (Hsp70) functions as a molecular chaperone.
  • Post-translational modifications regulate Hsp70 activity.
  • Pathogen kinases can target Hsp70 for inhibition.

Purpose of the Study:

  • To investigate the endogenous phosphorylation of Hsp70 at T495 in human cells.
  • To understand the role of Hsp70 phosphorylation in response to DNA damage.
  • To elucidate the mechanism by which Hsp70 phosphorylation affects cell cycle progression.

Main Methods:

  • Investigated endogenous Hsp70 phosphorylation in human cells using mass spectrometry.
  • Utilized yeast models with phosphomimetic and phosphonull Hsp70 variants.
  • Performed biochemical assays to analyze Hsp70 conformation and substrate binding.

Main Results:

  • Hsp70 phosphorylation at T495 occurs endogenously in human cells during DNA damage, especially when base excision repair is stressed.
  • This modification is cell cycle-dependent.
  • In yeast, Hsp70 variants mimicking or lacking phosphorylation at T495 disrupt G1/S cell cycle progression under normal and DNA-damaging conditions.
  • The T495E mutation results in an open-like Hsp70 conformation without impeding substrate binding.

Conclusions:

  • Dynamic Hsp70 phosphorylation at T495 is a conserved mechanism regulating the G1/S transition.
  • Hsp70 phosphorylation delays cell cycle progression in response to DNA damage.
  • Insights from pathogen-host interactions can reveal fundamental principles of cell biology.