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SUMO chain-induced dimerization activates RNF4.

Alejandro Rojas-Fernandez1, Anna Plechanovová2, Neil Hattersley2

  • 1Medical Research Council Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, Scotland DD1 5EH, UK; Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee, Scotland DD1 5EH, UK.

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Summary
This summary is machine-generated.

RNF4 E3 ligase activity is controlled by polySUMO substrates. High substrate levels activate RNF4, causing its dimerization, ubiquitylation, and subsequent degradation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Dimeric RING E3 ligases regulate protein substrates and ubiquitin-E2-conjugating enzyme complexes for catalysis.
  • RNF4 is an E3 ligase with a polySUMO-binding N-terminal domain and a C-terminal RING domain for dimerization.

Purpose of the Study:

  • To investigate the regulatory mechanisms controlling RNF4 E3 ligase activity.
  • To determine the role of polySUMO substrates in RNF4 activation and degradation.

Main Methods:

  • Ablation of SUMO protease SENP6 to increase polySUMO substrate concentration in vivo.
  • In vitro assays to assess RNF4 activity at different concentrations and in the presence of SUMO chains.

Main Results:

  • Accumulation of polySUMO chains in vivo triggers ubiquitin-mediated proteolysis of RNF4.
  • In vitro, RNF4 is monomeric and inactive at physiological concentrations.
  • SUMO chains activate RNF4 by promoting dimerization, leading to substrate ubiquitylation and RNF4 autoubiquitylation.

Conclusions:

  • RNF4 E3 ligase activity is directly dependent on the availability of its polySUMO substrates.
  • PolySUMO chain abundance regulates RNF4's activation, dimerization, and subsequent degradation, providing a feedback mechanism.