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Structural basis for the dynamic conformations of AP-4 and its association with ARF1
Yanghui Wang1,2, Wei Li1, Yunlong Qiu1,2
1State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China.
Nature Communications
|January 21, 2026
Summary
Adaptor protein 4 (AP-4) is a dynamic complex crucial for intracellular membrane trafficking. Its recruitment is regulated by ARF1, with conformational flexibility being key for efficient cargo transport and insights into neurodevelopmental disorders.
Area of Science:
- Cell Biology
- Molecular Biology
- Structural Biology
Background:
- Adaptor protein complexes (APs) mediate intracellular membrane trafficking.
- AP-4 is a non-clathrin-coated vesicle machinery essential for this process.
- ARF1 regulates AP-4 membrane recruitment, but the mechanism is unclear.
Purpose of the Study:
- To elucidate the structural mechanism of AP-4 membrane recruitment by ARF1.
- To investigate the conformational dynamics of AP-4.
- To understand the role of ARF1-AP-4 interactions in membrane trafficking.
Main Methods:
- Cryo-electron microscopy (cryo-EM) to determine structures of soluble AP-4 and the AP-4/ARF1 complex.
- Mutational analysis to assess the functional impact of interface disruption.
Main Results:
- AP-4 exists in a dynamic equilibrium between closed and open conformations.
- ARF1 binding causes minimal conformational changes in AP-4, which retains its flexibility.
- Mutations at the ARF1-AP-4 interface impair complex formation and ARF1-dependent recruitment.
- Conformational flexibility is vital for synergistic ARF1 and cargo engagement.
Conclusions:
- AP-4 is a conformationally dynamic complex regulated by ARF1 and cargo interactions.
- Disrupting AP-4 flexibility impairs membrane trafficking, offering insights into AP-4-related neurodevelopmental disorders.
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