Dataset Information

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

ABSTRACT: In eukaryotes, membrane contact sites (MCS) allow direct communication between organelles. Plants have evolved unique MCS, the plasmodesmata intercellular pores, which combine organelle tethering with regulation of cell-to-cell signalling, the molecular mechanisms of which remains unknown. Here, we identify Multiple C2 domains and Transmembrane region Proteins (MCTPs) as tethers that link the endoplasmic reticulum (ER) to the plasma membrane (PM) within plasmodesmata. We report that MCTPs, including MCTP3 and 4 recently identified as modulators of SHOOTMERISTEMLESS trafficking, are ER-anchored proteins that cluster at plasmodesmata. MCTPs insert into the ER via their transmembrane region whilst their C2 domains dock to the PM through interaction with anionic phospholipids. A mctp3/4 loss-of function mutant induces plant developmental defects while MCTP4 expression in a yeast .tether mutant partially restores ER-PM tethering. Our data suggest that MCTPs are unique membrane tethers controlling both ER-PM contacts and cell-cell signalling.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Max Kraner

LAB HEAD: Max Edmund Kraner

PROVIDER: PXD013999 | Pride | 2019-07-08

REPOSITORIES: Pride

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

Brault Marie L ML Petit Jules D JD Immel Françoise F Nicolas William J WJ Glavier Marie M Brocard Lysiane L Gaston Amèlia A Fouché Mathieu M Hawkins Timothy J TJ Crowet Jean-Marc JM Grison Magali S MS Germain Véronique V Rocher Marion M Kraner Max M Alva Vikram V Claverol Stéphane S Paterlini Andrea A Helariutta Ykä Y Deleu Magali M Lins Laurence L Tilsner Jens J Bayer Emmanuelle M EM

EMBO reports 20190709 8

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 ...[more]

PMID: 31286648

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