title: A family of membrane-shaping proteins at ER subdomains regulates pre-peroxisomal vesicle biogenesis.
abstract: Saccharomyces cerevisiae contains three conserved reticulon and reticulon-like proteins that help maintain ER structure by stabilizing high membrane curvature in ER tubules and the edges of ER sheets. A mutant lacking all three proteins has dramatically altered ER morphology. We found that ER shape is restored in this mutant when Pex30p or its homologue Pex31p is overexpressed. Pex30p can tubulate membranes both in cells and when reconstituted into proteoliposomes, indicating that Pex30p is a novel ER-shaping protein. In contrast to the reticulons, Pex30p is low abundance, and we found that it localizes to subdomains in the ER. We show that these ER subdomains are the sites where most preperoxisomal vesicles (PPVs) are generated. In addition, overproduction or deletion of Pex30p or Pex31p alters the size, shape, and number of PPVs. Our findings suggest that Pex30p and Pex31p help shape and generate regions of the ER where PPV biogenesis occurs.
authors.affiliation: Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
authors.forename: Amit S
authors.initials: AS
authors.lastname: Joshi
authors.affiliation: Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.|Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin 300071, China.
authors.forename: Xiaofang
authors.initials: X
authors.lastname: Huang
authors.affiliation: Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
authors.forename: Vineet
authors.initials: V
authors.lastname: Choudhary
authors.affiliation: University College London Institute of Ophthalmology, London EC1V 9EL, England, UK.
authors.forename: Tim P
authors.initials: TP
authors.lastname: Levine
authors.affiliation: Department of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.|Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin 300071, China.|National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Junjie
authors.identifier: http://orcid.org/0000-0003-4712-2243
authors.initials: J
authors.lastname: Hu
authors.affiliation: Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 prinzw@helix.nih.gov.
authors.forename: William A
authors.identifier: http://orcid.org/0000-0002-9053-2398
authors.initials: WA
authors.lastname: Prinz
mesh_terms: D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D049452:Green Fluorescent Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008954:Models, Biological; D009154:Mutation / Q000235:genetics; D001678:Organelle Biogenesis; D020675:Peroxisomes / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D022161:Transport Vesicles / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; D049452:Green Fluorescent Proteins