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A Structural Model for the Core Nup358-BicD2 Interface
James M Gibson1, Xiaoxin Zhao2, M Yusuf Ali3
1Department of Biological Sciences, Department of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY 12180, USA.
Biomolecules
|October 28, 2023
Summary
The dynein adaptor Bicaudal D2 (BicD2) binds to Nup358 via two interfaces, revealing structural mechanisms for cargo selection in neuronal development.
Area of Science:
- Cellular biology
- Structural biology
- Neuroscience
Background:
- Dynein motors drive essential minus-end-directed transport along microtubules.
- Bicaudal D2 (BicD2) is a key adaptor protein that links cellular cargo to the dynein motor.
- Nup358 is a cargo recognized by BicD2, crucial for nuclear positioning in differentiating brain progenitor cells.
Purpose of the Study:
- To elucidate the structural details of the BicD2-Nup358 interaction.
- To understand how BicD2 selects Nup358 cargo for dynein-mediated transport.
- To provide a structural basis for BicD2's role in brain development.
Main Methods:
- Computational modeling using AlphaFold2, HADDOCK, and ClusPro.
- Site-directed mutagenesis to probe the BicD2-Nup358 interface.
- Analysis of protein-protein interactions and structural interfaces.
Main Results:
- The Nup358 cargo-recognition α-helix binds BicD2 (residues 747-774) in an anti-parallel helical bundle, stabilized by salt bridges.
- A secondary interface involves an intrinsically disordered Nup358 region binding BicD2 (residues 774-800).
- This BicD2 region also binds Rab6, suggesting competition for cargo adaptors.
Conclusions:
- Established the structural basis for Nup358 cargo recognition by BicD2.
- Identified dual binding interfaces, including a novel interaction with an intrinsically disordered region.
- Highlighted the mechanism of cargo selection by BicD2, impacting neuronal development pathways.
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