Architecture and permeability of post-cytokinesis plasmodesmata lacking cytoplasmic sleeves

Nicolas, William J; Grison, Magali; Trépout, Sylvain; Gaston, Amélia; Fouché, Mathieu; Cordelières, Fabrice P.; Oparka, Karl J.; Tilsner, Jens; Brocard, Lysiane; Bayer, Emmanuelle

doi:10.1038/nplants.2017.82

Cited by 140 publications

(177 citation statements)

References 78 publications

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“…A survey of our refined proteome identified several members of the multiple C2 domains and transmembrane region proteins (MCTPs) family, namely AtMCTP3-7, AtMCTP9, AtMCTP10 and 14-16, as both abundant and highly enriched at plasmodesmata (Appendix Fig S1B, Appendix Table S1). In addition to being plasmodesmata-enriched proteins, our data also suggest that MCTPs are differentially regulated during the ER-PM tethering transition from post-cytokinetic to mature plasmodesmata [25] (Appendix Fig S2). Amongst the 47 plasmodesmal proteins differentially enriched, all MCTPs were more abundant (1.4-3.6 times) in type I (tight ER-PM contacts) compared with type II (open cytoplasmic sleeves) plasmodesmata (Appendix Fig S2).…”

Section: Identification Of Plasmodesmal Er-pm Tethering Candidatesmentioning

confidence: 70%

“…Plasmodesmata are structurally unique [22,23]. They contain a strand of ER, continuous through the pores, tethered extremely tightly (~10 nm) to the PM by spoke-like elements [24,25] whose function and identity are unknown. Inside plasmodesmata, specialised subdomains of the ER and the PM co-exist, each being characterised by a unique set of lipids and proteins, both critical for proper function [6,12,[26][27][28][29][30][31].…”

Section: Introductionmentioning

confidence: 99%

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Multiple C2 domains and transmembrane region proteins ( MCTP s) tether membranes at plasmodesmata

et al. 2019

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In eukaryotes, membrane contact sites ( MCS ) allow direct communication between organelles. Plants have evolved a unique type of MCS , inside intercellular pores, the plasmodesmata, where endoplasmic reticulum ( ER )–plasma membrane ( PM ) contacts coincide with regulation of cell‐to‐cell signalling. The molecular mechanism and function of membrane tethering within plasmodesmata remain unknown. Here, we show that the multiple C2 domains and transmembrane region protein ( MCTP ) family, key regulators of cell‐to‐cell signalling in plants, act as ER ‐ PM tethers specifically at plasmodesmata. We report that MCTP s are plasmodesmata proteins that insert into the ER via their transmembrane region while their C2 domains dock to the PM through interaction with anionic phospholipids. A Atmctp3/Atmctp4 loss of function mutant induces plant developmental defects, impaired plasmodesmata function and composition, while MCTP 4 expression in a yeast Δtether mutant partially restores ER ‐ PM tethering. Our data suggest that MCTP s are unique membrane tethers controlling both ER ‐ PM contacts and cell‐to‐cell signalling.

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Section: Identification Of Plasmodesmal Er-pm Tethering Candidatesmentioning

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Multiple C2 domains and transmembrane region proteins ( MCTP s) tether membranes at plasmodesmata

et al. 2019

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“…a). Consistent with the results of our study, a previous study using electron microscopy proposed a structural relationship between EPCS development and the cytoplasmic sleeve formation in PD (Nicolas et al ., ). Although some post‐cytokinesis PD lacked open cytoplasmic sleeves, there was no difference in GFP diffusion between mature cells and post‐cytokinesis cells.…”

Section: Discussionmentioning

confidence: 97%

Structural and functional relationships between plasmodesmata and plant endoplasmic reticulum–plasma membrane contact sites consisting of three synaptotagmins

et al. 2020

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Summary Synaptotagmin 1 (SYT1) has been recognised as a tethering factor of plant endoplasmic reticulum (ER)–plasma membrane (PM) contact sites (EPCSs) and partially localises to around plasmodesmata (PD). However, other components of EPCSs associated with SYT1 and functional links between the EPCSs and PD have not been identified. We explored interactors of SYT1 by immunoprecipitation and mass analysis. The dynamics, morphology and spatial arrangement of the ER in Arabidopsis mutants lacking the EPCS components were investigated using confocal microscopy and electron microscopy. PD permeability of EPCS mutants was assessed using a virus movement protein and free green fluorescent protein (GFP) as indicators. We identified two additional components of the EPCSs, SYT5 and SYT7, that interact with SYT1. The mutants of the three SYTs were defective in the anchoring of the ER to the PM. The ER near the PD entrance appeared to be weakly squeezed in the triple mutant compared with the wild‐type. The triple mutant suppressed cell‐to‐cell movement of the virus movement protein, but not GFP diffusion. We revealed major additional components of EPCS associated with SYT1 and suggested that the EPCSs arranged around the PD squeeze the ER to regulate active transport via PD.

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“…Additionally, the ER passes through the plasmodesmata, which are tiny channels that protrude into the cell wall and interconnect the cytoplasm of neighboring cells (Carr, 1976;Wright and Oparka, 2006). These structures are unique to plants and are crossed by a narrow tube-like structure, named desmotubule, which is derived from the ER (Quader and Zachariadis, 2006;Knox et al, 2015;Nicolas et al, 2017). As a result, the ER of each cell is interconnected to the neighboring cells through these channels, forming a virtually unique organelle whose extension is not delimited by the cell's boundaries.…”

Section: The Er Is a Pleomorphic Organelle Whose Morphology And Dynammentioning

confidence: 99%

Advances in Plant ER Architecture and Dynamics

Stefano

Brandizzí

2017

Plant Physiol.

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Architecture and permeability of post-cytokinesis plasmodesmata lacking cytoplasmic sleeves

Cited by 140 publications

References 78 publications

Multiple C2 domains and transmembrane region proteins ( MCTP s) tether membranes at plasmodesmata

Multiple C2 domains and transmembrane region proteins ( MCTP s) tether membranes at plasmodesmata

Structural and functional relationships between plasmodesmata and plant endoplasmic reticulum–plasma membrane contact sites consisting of three synaptotagmins

Advances in Plant ER Architecture and Dynamics

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