ArticleeLife2022
Coil-to-α-helix transition at the Nup358-BicD2 interface activates BicD2 for dynein recruitment.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Activation and regulation of the dynein-dynactin-NuMA complex.Nature chemical biology · 2026Article
- Synthetic cargo adaptors reveal molecular features that enhance dynein activation.Nature communications · 2026Article
- Cargo Recognition of Nesprin-2 by the Dynein Adapter Bicaudal D2 for a Nuclear Positioning Pathway That Is Important for Brain Development.Biochemistry · 2026Article
- Adaptor-mediated recruitment of three dyneins to dynactin enhances force generation.Nature cell biology · 2026Article
- The intracellular bacterium Orientia tsutsugamushi uses the autotransporter ScaC to activate BICD adaptors for dynein-based motility.Nature communications · 2025Article
- HIV-1 binds dynein directly to hijack microtubule transport machinery.Science advances · 2025Article
- ZYG-12/Hook's dual role as a dynein adaptor for early endosomes and nuclei is regulated by alternative splicing of its cargo binding domain.Molecular biology of the cell · 2025Article
- The nucleoporin Nup153 is the anchor for Kif1a during basal nuclear migration in brain progenitor cells.Cell reports · 2024Article
- Cargo adaptor identity controls the mechanism and kinetics of dynein activation.bioRxiv : the preprint server for biology · 2024Article
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- Molecular mechanism for recognition of the cargo adapter Rab6Life science alliance · 2024Article
- Positioning centrioles and centrosomes.The Journal of cell biology · 2024Review
- A Structural Model for the Core Nup358-BicD2 Interface.Biomolecules · 2023Article
- BICD2 phosphorylation regulates dynein function and centrosome separation in G2 and M.Nature communications · 2023Article
- TRAK adaptors regulate the recruitment and activation of dynein and kinesin in mitochondrial transport.Nature communications · 2023Article
- Role of Nesprin-2 and RanBP2 in BICD2-associated brain developmental disorders.PLoS genetics · 2023Article
- Article
- Workshop on RanBP2/Nup358 and acute necrotizing encephalopathy.Nucleus (Austin, Tex.) · 2022Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Nup358, a protein of the nuclear pore complex, facilitates a nuclear positioning pathway that is essential for many biological processes, including neuromuscular and brain development. Nup358 interacts with the dynein adaptor Bicaudal D2 (BicD2), which in turn recruits the dynein machinery to position the nucleus. However, the molecular mechanisms of the Nup358/BicD2 interaction and the activation of transport remain poorly understood. Here for the first time, we show that a minimal Nup358 domain activates dynein/dynactin/BicD2 for processive motility on microtubules. Using nuclear magnetic resonance titration and chemical exchange saturation transfer, mutagenesis, and circular dichroism spectroscopy, a Nup358 α-helix encompassing residues 2162-2184 was identified, which transitioned from a random coil to an α-helical conformation upon BicD2 binding and formed the core of the Nup358-BicD2 interface. Mutations in this region of Nup358 decreased the Nup358/BicD2 interaction, resulting in decreased dynein recruitment and impaired motility. BicD2 thus recognizes Nup358 through a 'cargo recognition α-helix,' a structural feature that may stabilize BicD2 in its activated state and promote processive dynein motility.
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