title: ER structure and function.
abstract: The ER forms a contiguous structure of interconnected sheets and tubules that spreads from the nuclear envelope to the cell cortex. Through its attachment to the cytoskeleton, the ER undergoes dynamic rearrangements, such as tubule extension and movement. ER shaping proteins (reticulons and DP1/Yop1p) play key roles in generating and maintaining the unique reticular morphology of the ER. Atlastin and its yeast homologue, Sey1p, mediate homotypic ER membrane fusion, which leads to the formation of new three-way junctions within the polygonal network. At these junctions, the Lunapark protein, Lnp1p, works in conjunction with the reticulons, DP1/Yop1p, and in antagonism to atlastin/Sey1p to maintain the network in a dynamic equilibrium. Defects in ER morphology have been linked to certain neurological disorders.
authors.affiliation: Department of Cellular and Molecular Medicine, Howard Hughes, Medical Institute, University of California at San Diego, La Jolla, CA 92093-0668, USA.
authors.forename: Shuliang
authors.initials: S
authors.lastname: Chen
authors.forename: Peter
authors.initials: P
authors.lastname: Novick
authors.forename: Susan
authors.initials: S
authors.lastname: Ferro-Novick
mesh_terms: D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008561:Membrane Fusion; D008565:Membrane Proteins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism; D009685:Nuclear Envelope / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism
chemical_list: D008565:Membrane Proteins