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Updated: Dec 28, 2025
07:53
Application of High-speed Super-resolution SPEED Microscopy in Live Primary Cilium
Published on: January 16, 2018
8.6K
Moving proteins along in the cilium.
Narcis Adrian Petriman1, Esben Lorentzen1
1Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Elife
|February 14, 2020
Summary
Structural analysis of the bovine and human BBSome complex reveals a necessary conformational change for its recruitment to the ciliary membrane, crucial for cellular function.
Area of Science:
- Cell Biology
- Structural Biology
- Biochemistry
Background:
- The BBSome is a large protein complex essential for cilia formation and function.
- Cilia play vital roles in various physiological processes, and their dysfunction is linked to numerous diseases.
Purpose of the Study:
- To elucidate the structural basis for BBSome recruitment to the ciliary membrane.
- To understand the conformational dynamics of the BBSome.
Main Methods:
- X-ray crystallography was used to determine the structures of the bovine and human BBSome.
- Comparative structural analysis was performed.
Main Results:
- The high-resolution structures of the bovine and human BBSome were resolved.
- A significant conformational change within the BBSome complex was identified as a prerequisite for ciliary membrane association.
Conclusions:
- The identified conformational change is a key regulatory mechanism for BBSome localization.
- Understanding this mechanism provides insights into ciliopathies and potential therapeutic targets.
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