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A recombinant BBSome core complex and how it interacts with ciliary cargo.

Björn Udo Klink1,2, Eldar Zent2, Puneet Juneja1

  • 1Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.

Elife
|November 24, 2017
PubMed
Summary

The BBSome protein complex binds to cellular receptors via a complex recognition mechanism, not solely through previously known targeting sequences. This finding clarifies how sensory proteins are transported to cilia.

Keywords:
BBSomeE. coliS.frugiperdabiochemistrybiophysicsciliary cargociliumhumanintraflagellar transportstructural biology

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Area of Science:

  • Cell biology
  • Molecular biology
  • Genetics

Background:

  • Cilia are crucial sensory organelles housing specific proteins like GPCRs.
  • The BBSome complex mediates the transport of these ciliary proteins.
  • BBSome dysfunction causes Bardet-Biedl syndrome, a serious ciliopathy.

Purpose of the Study:

  • To investigate the mechanistic details of ciliary targeting sequences (CTS) and BBSome binding.
  • To analyze the architecture of BBSome subcomplexes and their interactions with receptors.

Main Methods:

  • Heterologous expression of BBSome subcomplexes.
  • Biochemical analysis of receptor binding to the BBSome.

Main Results:

  • A stable heterohexameric BBSome complex was identified.
  • This complex binds GPCRs through interactions partially distinct from known CTS.
  • Arl6•GTP did not influence BBSome-receptor interactions, suggesting it's not directly involved in cargo transport.

Conclusions:

  • Ciliary protein targeting involves a more intricate recognition mechanism than previously understood.
  • The BBSome's interaction with GPCRs is complex and not fully explained by current CTS models.
  • Arl6's role in cargo loading/unloading appears indirect.