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Multiple C2 domains and Transmembrane region Proteins (MCTPs) tether membranes at plasmodesmata

Research output: Contribution to journalArticlepeer-review


Marie L. Brault, Jules D. Petit, Françoise Immel, William J. Nicolas, Marie Glavier, Lysiane Brocard, Amèlia Gaston, Mathieu Fouché, Timothy J. Hawkins, Jean-Marc Crowet, Magali S. Grison, Véronique Germain, Marion Rocher, Max Kraner, Vikram Alva, Stéphane Claverol, Andrea Paterlini, Ykä Helariutta, Magali Deleu, Laurence Lins & 2 more Jens Tilsner, Emmanuelle M. Bayer

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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 MCTPs 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 MCTP4 expression in a yeast Δtether mutant partially restores ER‐PM tethering. Our data suggest that MCTPs are unique membrane tethers controlling both ER‐PM contacts and cell‐to‐cell signalling.


Original languageEnglish
Article numbere47182
Number of pages26
JournalEMBO Reports
Issue number8
Early online date9 Jul 2019
Publication statusPublished - 1 Aug 2019

    Research areas

  • Plasmodesmata, Intracellular communication in plants, ER-PM membrane contact sites, Multiple C2 domains transmembrane region proteins

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