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Structure and interactions of the endogenous human Commander complex.

Saara Laulumaa1, Esa-Pekka Kumpula1, Juha T Huiskonen2

  • 1Institute of Biotechnology, Helsinki Institute of Life Science HiLIFE, University of Helsinki, Helsinki, Finland.

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|March 8, 2024
PubMed
Summary

The Commander complex

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Protein Complexes

Background:

  • The Commander complex, a 16-protein assembly, is crucial for cell homeostasis, cell cycle, and immune response.
  • It comprises copper-metabolism Murr1 domain proteins (COMMD1-10), CCDC22, CCDC93, DENND10, and the Retriever subcomplex (VPS26C, VPS29, VPS35L).
  • Dysregulation of the Commander complex is linked to various diseases.

Purpose of the Study:

  • To elucidate the structure and key interactions of the endogenous human Commander complex.
  • To define the precise composition and architecture of the Commander complex.
  • To investigate the functional implications of the Commander complex in cellular processes.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the complex's structure.
  • Mass spectrometry-based proteomics was utilized to establish its composition and interactions.
  • Biochemical assays were performed to validate key protein interfaces.

Main Results:

  • The Commander complex features a stable core of COMMD1-10 proteins.
  • An effector module containing DENND10 and the Retriever subcomplex is present.
  • CCDC22 and CCDC93 act as scaffolds, integrating the core and effector modules.
  • Major interaction interfaces within the complex were identified.

Conclusions:

  • The study reveals the detailed architecture of the human Commander complex.
  • Findings clarify the complex's roles in intracellular transport.
  • A significant association between the Commander complex and cilium assembly, centrosome, and centriole functions was uncovered.