Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning

Daniel Rozbesky (), Ross A. Robinson, Vitul Jain, Max Renner, Tomas Malinauskas, Karl Harlos, Christian Siebold and E. Yvonne Jones ()
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Daniel Rozbesky: University of Oxford
Ross A. Robinson: University of Oxford
Vitul Jain: University of Oxford
Max Renner: University of Oxford
Tomas Malinauskas: University of Oxford
Karl Harlos: University of Oxford
Christian Siebold: University of Oxford
E. Yvonne Jones: University of Oxford

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Semaphorin ligands and their plexin receptors are one of the major cell guidance factors that trigger localised changes in the cytoskeleton. Binding of semaphorin homodimer to plexin brings two plexins in close proximity which is a prerequisite for plexin signalling. This model appears to be too simplistic to explain the complexity and functional versatility of these molecules. Here, we determine crystal structures for all members of Drosophila class 1 and 2 semaphorins. Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond. Unexpectedly, our structural and biophysical data show Sema1b is a monomer suggesting that semaphorin function may not be restricted to dimers. We demonstrate that semaphorins can form heterodimers with members of the same semaphorin class. This heterodimerization provides a potential mechanism for cross-talk between different plexins and co-receptors to allow fine-tuning of cell signalling.

Date: 2019
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DOI: 10.1038/s41467-019-11683-y

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