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

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Brault, Marie | Petit, Jules | Immel, Françoise | Nicolas, William | Glavier, Marie | Brocard, Lysiane | Gaston, Amélia | Fouche, Mathieu | Hawkins, Timothy, J | Crowet, Jean-Marc | Grison, Magali | Germain, Véronique | Rocher, Marion | Kraner, Max | Alva, Vikram | Claverol, Stéphane | Paterlini, Andrea | Helariutta, Ykä | Deleu, Magali | Lins, Laurence | Tilsner, Jens | Bayer, Emmanuelle, Maria

Edité par CCSD ; EMBO Press -

UMR BFP - Equipe OrFE - Equipe A3C. International audience. 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 endoplas-mic 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 trans-membrane region protein (MCTP) family, key regulators of cell-to-cell signalling in plants, act as ER-PM tethers specifically at plasmodes-mata. 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 Dtether 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.

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