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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
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.
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.
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