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Related Experiment Videos

Structural basis for endosomal targeting by the Bro1 domain.

Jaewon Kim1, Sujatha Sitaraman, Aitor Hierro

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, U.S. Department of Health and Human Services, Bethesda, Maryland 20892, USA.

Developmental Cell
|June 7, 2005
PubMed
Summary

The Bro1 domain, crucial for protein sorting to endosomes, has its structure and function revealed. This research defines how Bro1 binds to ESCRT-III subunit Snf7, enabling protein targeting.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Mechanisms

Background:

  • Late endosomal protein sorting relies on ESCRT complexes and associated proteins like Alix and Bro1.
  • A conserved Bro1 domain in these proteins is vital but poorly characterized.

Purpose of the Study:

  • To determine the structure, boundaries, and function of the Bro1 domain.
  • To elucidate the mechanism of Bro1 recruitment to late endosomes and its interaction with ESCRT components.

Main Methods:

  • X-ray crystallography was used to determine the structure of the Bro1 domain.
  • Biochemical assays were employed to study the binding of Bro1 to the ESCRT-III subunit Snf7.

Main Results:

  • The crystal structure of the Bro1 domain (367 residues) was solved, revealing a boomerang-like shape with a triple tetratricopeptide repeat substructure.

Related Experiment Videos

  • The extended Bro1 domain is essential for binding to Snf7 and recruiting Bro1 to late endosomes.
  • Snf7 binds to a specific hydrophobic patch on Bro1, critical for complex formation and protein sorting.

    • Conclusions:

    • The study defines the structure and function of the Bro1 domain.
    • A conserved mechanism for targeting Bro1 domain-containing proteins to endosomes via Snf7 interaction is established.