Identification of nuclear pore proteins at plasmodesmata
Schladt, T. M.; Miras, M.; Ejike, J. O.; Pottier, M.; Xi, L.; Restrepo, A.; Nakamura, M.; Puetz, N.; Haensch, S.; Gao, C.; Engelhorn, J.; Dickmanns, M.; Davis, G.; Dalal, A.; Gombos, S.; Lange, R.; Simon, R.; Schulze, W. X.; Frommer, W. B.
Show abstract
Plasmodesmata (PD) mediate intercellular exchange of small molecules, RNAs and proteins between plant cells with an apparent exclusion limit for passive non-specific transport, and transport of specific cargo mediated by mediators. PD and nuclear pore complexes (NPC) are nanometer sized micropores with strikingly similar properties. Cargo translocation through NPC is mediated by phase separating FG-nucleoporins (FG-NUP). Here, bioinformatics, proteomics and fluorescence imaging identified FG-NUPs at PD. Transient expression of GFP fusions at low and intermediate expression levels supported dual localization of 12 NUPs to NPC and PD. Structured illumination microscopy detected the transmembrane anchor NUP CPR5 close to orifices of PD. cpr5 mutants showed reduced intercellular short-root (SHR) transport. However, transport defects cannot be excluded due to indirect effects in the mutants. Identification of FG-NUPs at PD is consistent with the recruitment of NUPs to form a PD pore gating complex consistent with phase separation domains as diffusion barriers at PD. Further analyses will be required to determine whether NUPs are bona fide PD components, or accumulate at PD in certain conditions, or may serve intermediate NPC storage.
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