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Development and characterisation of SMURF2-targeting modifiers.

Dhanoop Manikoth Ayyathan1, Gal Levy-Cohen1, Moran Shubely2

  • 1Laboratory of Molecular and Cellular Cancer Biology, Azrieli Faculty of Medicine, Bar-Ilan University, Safed, Israel.

Journal of Enzyme Inhibition and Medicinal Chemistry
|January 12, 2021
PubMed
Summary
This summary is machine-generated.

Researchers developed synthetic molecules to target the SMURF2 E3 ubiquitin ligase, promoting its degradation. This approach accelerates cell growth and enhances sensitivity to chemotherapy drugs like etoposide.

Keywords:
SMURF2autoubiquitinationpeptidespeptidomimetics

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • SMURF2, a C2-WW-HECT-domain E3 ubiquitin ligase, regulates key cellular functions.
  • No specific modulators for SMURF2 have been previously developed.

Purpose of the Study:

  • To design and evaluate synthetic peptides and peptidomimetics targeting SMURF2.
  • To investigate SMURF2 modulation via disruption of intramolecular C2-HECT domain interactions.
  • To assess the impact of SMURF2 targeting on cellular processes and drug sensitivity.

Main Methods:

  • Generation and screening of SMURF2-targeting synthetic peptides and peptidomimetics.
  • In vitro and in cellulo assays to determine molecular effects.
  • Utilisation of SMURF2-specific shRNAs for comparative analysis.
  • Assessment of cell growth and cytotoxicity in combination treatments.

Main Results:

  • Developed SMURF2 modulators effective at nanomolar concentrations.
  • Demonstrated that SMURF2 targeting accelerates cell growth in a context-dependent manner.
  • Showed that SMURF2 inactivation potentiates etoposide-induced cytotoxicity.

Conclusions:

  • SMURF2 is druggable through induction of its autoubiquitination and turnover.
  • Targeting SMURF2 offers a potential strategy to enhance anticancer drug efficacy.