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Co-adaptor driven assembly of a CUL3 E3 ligase complex.

David Akopian1, Colleen A McGourty1, Michael Rapé2

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|February 5, 2022
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Summary

Cullin-RING ligases (CRLs) assemble via substrate adaptors and cullins. A co-adaptor, PEF1-ALG2, initiates CRL3 formation and couples substrate recruitment to ubiquitylation, controlling development.

Keywords:
ALG2CAND1CUL3KLHL12PEF1SEC31adaptor exchangemonoubiquitylationubiquitin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Cullin-RING ligases (CRLs) are crucial ubiquitylation enzymes.
  • CRLs consist of a cullin scaffold and diverse substrate adaptors.
  • The assembly of CRLs is essential for signal transduction but poorly understood.

Purpose of the Study:

  • To investigate the regulation of CRL complex formation.
  • To elucidate the role of co-adaptors in CRL assembly and function.
  • To understand how CRL assembly is coupled to substrate recognition.

Main Methods:

  • Utilized CUL3KLHL12 as a model system.
  • Investigated the function of the co-adaptor PEF1-ALG2.
  • Examined the process of CRL3 formation and stabilization.

Main Results:

  • PEF1-ALG2 initiates CRL3 formation by releasing KLHL12 from an inhibitor at the ER.
  • Co-adaptor monoubiquitylation stabilizes the CRL3 enzyme.
  • The co-adaptor links substrate recruitment to ubiquitylation.

Conclusions:

  • CRL assembly is a tightly regulated process.
  • Specific CRL regulators, like co-adaptors, cooperate with general adaptor exchange.
  • This coordinated mechanism establishes E3 ligase complexes controlling metazoan development.