Identification of nuclear pore proteins at plasmodesmata: potential role in intercellular transport?
Moritz SchladtiD, Manuel MirasiD, Jona Obinna EjikeiD, Mathieu PottieriD, Lin XiiD, Andrea Restrepo-EscobariD, Masayoshi NakamuraiD, Niklas PütziD, Sebastian HänschiD, Chen GaoiD, Julia EngelhorniD, Marcel DickmannsiD, Gwendolyn V. DavisiD, Ahan DalaliD, Sven GombosiD, Ronja LangeiD, Rüdiger GW SimoniD, Waltraud X. SchulzeiD, Wolf Bernd FrommeriD
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.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 2
- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Nuclear Pore Transport: Toward an Integrated Perspective
Luca L. Lanzanò, Francesco Cardarelli·bioRxiv·Sep 18, 2025
- Deciphering the conformations and dynamics of FG-nucleoporins in situ
M. Yu, M. Heidari, … E. A. Lemke·bioRxiv·Jul 7, 2022
- Kap-centric Nsp1-mediated nuclear transport at full amino-acid resolution
Maurice Dekker, Hendrik W. de Vries, … Patrick R. Onck·Nature CommunicationsPeer-reviewed·Dec 12, 2025
- Intrinsically disordered nuclear pore proteins show ideal-polymer morphologies and dynamics
L. K. Davis, I. J. Ford, … B. Hoogenboom·bioRxiv·Sep 17, 2019
- Crowding-induced phase separation of nuclear transport receptors in FG nucleoporin assemblies
L. K. Davis, I. J. Ford, B. W. Hoogenboom·bioRxiv·Jul 24, 2021
- COMPUTATIONAL STUDIES OF CARGO TRANSPORT THROUGH THE NUCLEAR PORE COMPLEX
Sanjeev K. Gautam, Rozita Laghaei, … Rob D. Coalson·bioRxiv·Feb 24, 2026