Specialised membrane domains of plasmodesmata, plant intercellular nanopores

Specialised membrane domains of plasmodesmata, plant intercellular nanopores

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Plasmodesmata (PD) are plant-specific intercellular nanopores defined by specialised domains of the plasma membrane (PM) and the endoplasmic reticulum (ER), both of which contain unique proteins, and probably different lipid compositions than the surrounding bulk membranes. The PD membranes form concentric tubules with a minimal outer diameter of only 50 nm, and the central ER strand constricted to ~10-15 nm, representing one of the narrowest stable membrane tubules in nature. This unique membrane architecture poses many biophysical, structural and functional questions. PM continuity across PD raises the question as to how a locally confined membrane site is established and maintained at PD. There is increasing evidence that the PM within PD may be enriched in membrane a€˜raftsa€™ or TET web domains. Lipid rafts often function as signalling platforms, in line with the emerging view of PD as central players in plant defense responses. Lipid-lipid immiscibility could also provide a mechanism for membrane sub- compartmentalisation at PD. Intricate connections of the PM to the wall and the underlying cytoskeleton and ER may anchor the specialised domains locally. The ER within PD is even more strongly modified. Its extreme curvature suggests that it is stabilised by densely packed proteins, potentially members of the reticulon family that tubulate the cortical ER. The diameter of the constricted ER within PD is similar to membrane stalks in dynamin-mediated membrane fission during endocytosis and may need to be stabilised against spontaneous rupture. The function of this extreme membrane constriction, and the reasons why the ER is connected between plant cells remain unknown. Whilst the technically challenging search for the protein components of PD is ongoing, there has been significant recent progress in research on biological membranes that could benefit our understanding of PD function. With this Research Topic, we therefore aim to bring together researchers in the PD field and those in related areas, such as membrane biophysics, membrane composition and fluidity, protein-lipid interactions, lateral membrane heterogeneity, lipid rafts, membrane curvature, and membrane fusion/fission. We wish to address questions such as: - What mechanisms restrict lateral mobility of proteins and lipids along the PD membranes? - How can specific proteins be targeted to and turned over from membrane domains with restricted lateral access? - What elements (lipids, proteins, membrane curvature, packing order, thickness etc.) may contribute to the identity of PD membranes? - How do the structural and functional features of PD compare to other ER-PM contact sites? - How is the high curvature of the PD ER stabilised and what are possible functions of such a tightly constricted membrane tubule? - Do PD need to be prevented from spontaneous collapse and sealing? - What technologies are available to address these questions that can underpin PD research? We welcome interested individuals to contribute their expertise and develop new hypotheses on the particular biological and biophysical questions posed by PD. We are particularly looking for articles (Original Research Articles, Technical Advances and State-of-the-Art reviews) that would expand on or challenge current perceptions of PD and stimulate discussion.Plant cells do not possess ATL, but a family of similar GTPases, named root hair defective 3 (RHD3), are likely the functional orthologs of ATLs. ... INTRODUCTION The endoplasmic reticulum (ER) is the origin of the endomembrane system in eukaryotic cells. ... Morphologically, the ER membranes can adopt a tubular shape or form flattened cisternal structures, called ER sheets (Shibata et al., 2006).

Title:Specialised membrane domains of plasmodesmata, plant intercellular nanopores
Author: Jens Tilsner, Emmanuelle Bayer, Sébastien MONGRAND, Lesley Torrance
Publisher:Frontiers E-books - 2014-12-17

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