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Updated: Dec 18, 2025

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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SIRT7 Deacetylates STRAP to Regulate p53 Activity and Stability.

Miao Yu1,2, Xiaoyan Shi3, Mengmeng Ren1

  • 1Department of Medical Genetics, Center for Medical Genetics, Peking University Health Science Center, Beijing 100191, China.

International Journal of Molecular Sciences
|June 13, 2020
PubMed
Summary

Serine-threonine kinase receptor-associated protein (STRAP) acetylation by CBP and SIRT7 regulates p53 activity. This acetylation influences p53-mediated cell cycle arrest and apoptosis following stress.

Keywords:
5-FU treatmentSIRT7STRAPacetylationp53

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Serine-threonine kinase receptor-associated protein (STRAP) is a key regulator of TGF-β and p53 signaling pathways.
  • STRAP's role in cell proliferation and apoptosis under stress conditions is critical.
  • Understanding post-translational modifications of STRAP is essential for deciphering its regulatory functions.

Purpose of the Study:

  • To investigate the role of STRAP acetylation in p53-mediated cellular responses.
  • To identify the enzymes responsible for STRAP acetylation and deacetylation.
  • To elucidate how STRAP acetylation impacts p53 activation and stability.

Main Methods:

  • Site-directed mutagenesis to create hypo- and hyperacetylation mutants (3KR/3KQ) of STRAP.
  • In vitro and in vivo assays to assess STRAP acetylation by CREB-binding protein (CBP) and deacetylation by sirtuin7 (SIRT7).
  • Western blot analysis and immunofluorescence to evaluate p53 stabilization, nuclear translocation of STRAP, and STRAP acetylation levels after 5-fluorouracil (5-FU) treatment.

Main Results:

  • STRAP is acetylated at lysines 147, 148, and 156 by CBP and deacetylated by SIRT7.
  • STRAP acetylation status (3KR/3KQ mutants) significantly affects p53 activation and stabilization.
  • 5-FU treatment induces STRAP nuclear translocation and promotes its acetylation, linking cellular stress to STRAP modification.
  • STRAP acetylation directly influences p53 activity and stability, connecting the p53 and SIRT7 pathways.

Conclusions:

  • STRAP acetylation is a crucial regulatory mechanism for p53-mediated cell cycle arrest and apoptosis.
  • The balance between CBP-mediated acetylation and SIRT7-mediated deacetylation of STRAP fine-tunes p53 signaling.
  • These findings reveal a novel link between STRAP, SIRT7, and p53, offering potential therapeutic targets for stress-induced cellular responses.