caa a22 4500 44584020X CHVBK 20180317145341.0 cr unu---uuuuu 170323e20110101xx s 000 0 eng 10.1007/s00709-010-0217-6 doi (NATIONALLICENCE)springer-10.1007/s00709-010-0217-6 Plasmodesmata viewed as specialised membrane adhesion sites [Elektronische Daten] [Jens Tilsner, Khalid Amari, Lesley Torrance] A significant amount of work has been expended to identify the elusive components of plasmodesmata (PD) to help understand their structure, as well as how proteins are targeted to them. This review focuses on the role that lipid membranes may play in defining PD both structurally and as subcellular targeting addresses. Parallels are drawn to findings in other areas of research which focus on the lateral segregation of membrane domains and the generation of three-dimensional organellar shapes from flat lipid bilayers. We conclude that consideration of the protein-lipid interactions in cell biological studies of PD components and PD-targeted proteins may yield new insights into some of the many open questions regarding these unique structures. Springer-Verlag, 2010 Plasmodesma nationallicence Protein-lipid interaction nationallicence Lipid rafts nationallicence Membrane curvature nationallicence Endomembranes nationallicence Subcellular targeting nationallicence DRM : Detergent resistant membrane nationallicence DT : Desmotubule nationallicence EM : Electron microscopy nationallicence ER : Endoplasmic reticulum nationallicence GFP : Green fluorescent protein nationallicence GPI : Glycosyl phosphatidyl inositol nationallicence Ld : Liquid-disordered nationallicence Lo : Liquid-ordered nationallicence MP : Movement protein nationallicence PD : Plasmodesma(ta) nationallicence PDLP : Plasmodesmata-located protein nationallicence PDCB : Pd callose binding protein nationallicence PIP : Phosphatidylinositol phosphate nationallicence PMTV : Potato mop-top virus nationallicence PVX : Potato virus X nationallicence So : Solid-ordered nationallicence TMD : Transmembrane domain nationallicence TMV : Tobacco mosaic virus nationallicence Tilsner Jens Institute of Molecular Plant Sciences, University of Edinburgh, Mayfield Road, EH9 3JH, Edinburgh, UK aut Amari Khalid Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 12 Rue du Général Zimmer, 67084, Strasbourg, France aut Torrance Lesley Plant Pathology Department, Scottish Crop Research Institute, DD2 5DA, Invergowrie, Dundee, UK aut Protoplasma Springer Vienna 248/1(2011-01-01), 39-60 0033-183X 248:1<39 2011 248 709 https://doi.org/10.1007/s00709-010-0217-6 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00709-010-0217-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tilsner Jens Institute of Molecular Plant Sciences, University of Edinburgh, Mayfield Road, EH9 3JH, Edinburgh, UK aut NATIONALLICENCE 700 1- Amari Khalid Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, 12 Rue du Général Zimmer, 67084, Strasbourg, France aut NATIONALLICENCE 700 1- Torrance Lesley Plant Pathology Department, Scottish Crop Research Institute, DD2 5DA, Invergowrie, Dundee, UK aut NATIONALLICENCE 773 0- Protoplasma Springer Vienna 248/1(2011-01-01), 39-60 0033-183X 248:1<39 2011 248 709 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer