ArticleBiophysical journal2019
Solution Structure of C. elegans UNC-6: A Nematode Paralogue of the Axon Guidance Protein Netrin-1.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Structural insights into the formation of repulsive netrin guidance complexes.Science advances · 2024Article
- Investigation of dynamic solution interactions between NET-1 and UNC-5B by multi-wavelength analytical ultracentrifugation.European biophysics journal : EBJ · 2023Article
- The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation.Nature communications · 2023Article
- Homogenous overexpression of the extracellular matrix protein Netrin-1 in a hollow fiber bioreactor.Applied microbiology and biotechnology · 2021Article
- Neural Tissue Homeostasis and Repair Is Regulated via CS and DS Proteoglycan Motifs.Frontiers in cell and developmental biology · 2021Review
- Structural and Hydrodynamic Characterization of Dimeric Human Oligoadenylate Synthetase 2.Biophysical journal · 2020Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
UNCoordinated-6 (UNC-6) was the first member of the netrin family to be discovered in Caenorhabditis elegans. With homology to human netrin-1, it is a key signaling molecule involved in directing axon migration in nematodes. Similar to netrin-1, UNC-6 interacts with multiple receptors (UNC-5 and UNC-40, specifically) to guide axon migration in development. As a result of the distinct evolutionary path of UNC-6 compared to vertebrate netrins, we decided to employ an integrated approach to study its solution behavior and compare it to the high-resolution structure we previously published on vertebrate netrins. Dynamic light scattering and analytical ultracentrifugation on UNC-6 (with and without its C-domain) solubilized in a low-ionic strength buffer suggested that UNC-6 forms high-order oligomers. An increase in the buffer ionic strength resulted in a more homogeneous preparation of UNC-6, that was used for subsequent solution x-ray scattering experiments. Our biophysical analysis of UNC-6 ΔC solubilized in a high-ionic strength buffer suggested that it maintains a similar head-to-stalk arrangement as netrins -1 and -4. This phenomenon is thought to play a role in the signaling behavior of UNC-6 and its ability to move throughout the extracellular matrix.
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Registered trials
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