Curvature induction and membrane remodeling by FAM134B reticulon homology domain assist selective ER-phagy.
Autophagy
Cell Line, Tumor
Cell Membrane
/ metabolism
Endoplasmic Reticulum
/ metabolism
Humans
Intracellular Signaling Peptides and Proteins
Liposomes
/ metabolism
Membrane Proteins
/ genetics
Microscopy, Electron
Models, Molecular
Molecular Dynamics Simulation
Neoplasm Proteins
/ genetics
Organelle Shape
/ genetics
Protein Domains
Protein Transport
/ genetics
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
30 05 2019
30 05 2019
Historique:
received:
20
08
2018
accepted:
25
04
2019
entrez:
1
6
2019
pubmed:
31
5
2019
medline:
18
6
2019
Statut:
epublish
Résumé
FAM134B/RETREG1 is a selective ER-phagy receptor that regulates the size and shape of the endoplasmic reticulum. The structure of its reticulon-homology domain (RHD), an element shared with other ER-shaping proteins, and the mechanism of membrane shaping remain poorly understood. Using molecular modeling and molecular dynamics (MD) simulations, we assemble a structural model for the RHD of FAM134B. Through MD simulations of FAM134B in flat and curved membranes, we relate the dynamic RHD structure with its two wedge-shaped transmembrane helical hairpins and two amphipathic helices to FAM134B functions in membrane-curvature induction and curvature-mediated protein sorting. FAM134B clustering, as expected to occur in autophagic puncta, amplifies the membrane-shaping effects. Electron microscopy of in vitro liposome remodeling experiments support the membrane remodeling functions of the different RHD structural elements. Disruption of the RHD structure affects selective autophagy flux and leads to disease states.
Identifiants
pubmed: 31147549
doi: 10.1038/s41467-019-10345-3
pii: 10.1038/s41467-019-10345-3
pmc: PMC6542808
doi:
Substances chimiques
Intracellular Signaling Peptides and Proteins
0
Liposomes
0
Membrane Proteins
0
Neoplasm Proteins
0
RETREG1 protein, human
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2370Subventions
Organisme : Alexander von Humboldt-Stiftung (Alexander von Humboldt Foundation)
ID : Sofja Kovalevskaja Award
Pays : International
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : SFB 1177
Pays : International
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 259130777
Pays : International
Organisme : EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council)
ID : 742720 UbBAC,
Pays : International
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