Disease resistance through impairment of α-SNAP–NSF interaction and vesicular trafficking by soybean Rhg1

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 113; no. 47; pp. E7375 - E7382
• Main Authors: Bayless, Adam M., Smith, John M., Song, Junqi, McMinn, Patrick H., Teillet, Alice, August, Benjamin K., Bent, Andrew F.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 22.11.2016
• Series: PNAS Plus
• Subjects: Animals; Biological Sciences; Disease Resistance; Glycine max - genetics; Glycine max - metabolism; Glycine max - parasitology; Mutation; N-Ethylmaleimide-Sensitive Proteins - metabolism; Nematoda - physiology; Plant Diseases - parasitology; Plant Proteins - genetics; Plant Proteins - metabolism; PNAS Plus; Protein Binding; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - genetics; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - metabolism; Transport Vesicles - metabolism; plant disease resistance; soybean cyst nematode; α-SNAP; Rhg1

α-SNAP [soluble NSF (N-ethylmaleimide–sensitive factor) attachment protein] and NSF proteins are conserved across eukaryotes and sustain cellular vesicle trafficking by mediating disassembly and reuse of SNARE protein complexes, which facilitate fusion of vesicles to target membranes. However, certa...