title: Endoplasmatic reticulum shaping by generic mechanisms and protein-induced spontaneous curvature.
abstract: The endoplasmatic reticulum (ER) comprises flattened vesicles (cisternae) with worm holes dubbed with ribosomes coexisting with a network of interconnected tubes which can extend to the cell periphery or even penetrate nerve axons. The coexisting topologies enclose a continuous luminal space. The complex ER topology is specifically controlled by a group of ER-shaping proteins often called reticulons (discovered by the group of Tom Rapoport). They include atlastin, reticulon, REEP and the MT severing protein spastin. A generic ER shape controlling factor is the necessity to maximize the area-to-volume ratio of ER membranes in the highly crowded cytoplasmic space. I present a model of the ER-shaping function of the reticulons based on the Helfrich bending elasticity concept of soft shell shape changes. Common structural motifs of the reticulons are hydrophobic sequences forming wedge shaped hairpins which penetrate the lipid bilayer of the cell membranes. The wedge-like hydrophobic anchors can both induce the high curvature of the tubular ER fraction and ensure the preferred distribution of the reticulons along the tubules. Tubular junctions may be stabilized by the reticulons forming two forceps twisted by 90°. The ER extensions to the cell periphery and the axons are mediated by coupling of the tubes to the microtubules which is mediated by REEP and spastin. At the end I present a model of the tension driven homotype fusion of ER-membranes by atlastin, based on analogies to the SNARE-complexin-SNARE driven heterotype fusion process.
authors.affiliation: Physics Department, Technical University of Munich, James Franck Str.1, D85747 Garching, Germany. Electronic address: sackmann@ph.tum.de.
authors.forename: Erich
authors.initials: E
authors.lastname: Sackmann
mesh_terms: D000818:Animals; D055592:Biophysical Phenomena; D004721:Endoplasmic Reticulum / Q000737:chemistry* / Q000201:enzymology / Q000378:metabolism; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D053140:Organelle Shape; D013499:Surface Properties
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins
keywords: Atlastin; Curvature elasticity concept of biomembrane functions; Endoplasmatic reticulum shaping proteins; Lipid protein interaction; Membrane fusion; Membrane microtubule coupling; Reticulons; Spastin