Membrane Asymmetry Imposes Directionality on Lipid Droplet Emergence from the ER
| Autor: | Pedro Carvalho, Sihui Wang, Rainer D. Beck, Luca Monticelli, Joana Veríssimo Ferreira, Dalila Ajjaji, Mathias Beller, Errin Johnson, Abdou Rachid Thiam, Aymeric Chorlay, Mohyeddine Omrane, Kalthoum Ben M'barek |
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| Přispěvatelé: | Microfluidique, Émulsion et Biologie, Laboratoire de physique de l'ENS - ENS Paris (LPENS (UMR_8023)), École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Université Paris Diderot - Paris 7 (UPD7)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Université Paris Diderot - Paris 7 (UPD7), Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Sir William Dunn School of Pathology [Oxford], University of Oxford [Oxford], Universität Heidelberg [Heidelberg], Institute for Mathematical Modeling of Biological Systems [Düsseldorf], Heinrich Heine Universität Düsseldorf = Heinrich Heine University [Düsseldorf], Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris (FRDPENS), Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)-Université Paris Diderot - Paris 7 (UPD7)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris (FRDPENS), Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)-Université Paris Diderot - Paris 7 (UPD7)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Heinrich-Heine-Universität Düsseldorf [Düsseldorf] |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Membrane asymmetry
Carcinoma Hepatocellular [SDV]Life Sciences [q-bio] Plasma protein binding Saccharomyces cerevisiae Biology Endoplasmic Reticulum General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Lipid droplet Organelle Cytosolic lipid droplets Directionality Animals Humans Molecular Biology Cells Cultured Phospholipids ComputingMilieux_MISCELLANEOUS 030304 developmental biology 0303 health sciences Bilayer Cell Membrane Liver Neoplasms Membrane Proteins Cell Biology Lipid Droplets Directional budding Cytosol Membrane Biophysics Drosophila lipids (amino acids peptides and proteins) 030217 neurology & neurosurgery Developmental Biology Lumen (unit) |
| Zdroj: | Developmental Cell Developmental Cell, Elsevier, 2019, 50 (1), pp.25-42.e7. ⟨10.1016/j.devcel.2019.05.003⟩ |
| ISSN: | 1534-5807 |
| Popis: | During energy bursts, neutral lipids fabricated within the ER bilayer demix to form lipid droplets (LDs). LDs bud off mainly in the cytosol where they regulate metabolism and multiple biological processes. They indeed become accessible to most enzymes and can interact with other organelles. How such directional emergence is achieved remains elusive. Here, we found that this directionality is controlled by an asymmetry in monolayer surface coverage. Model LDs emerge on the membrane leaflet of higher coverage, which is improved by the insertion of proteins and phospholipids. In cells, continuous LD emergence on the cytosol would require a constant refill of phospholipids to the ER cytosolic leaflet. Consistent with this model, cells deficient in phospholipids present an increased number of LDs exposed to the ER lumen and compensate by remodeling ER shape. Our results reveal an active cooperation between phospholipids and proteins to extract LDs from ER. |
| Databáze: | OpenAIRE |
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