Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes

A single particle cryo-EM reconstruction of an ∼160-kD N-terminal fragment of the lipid transport protein VPS13 reveals an ∼160-Å long channel lined with hydrophobic residues suitable for solubilizing multiple lipid fatty acid moieties. The structure suggests that VPS13 and related proteins, like th...

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Detalles Bibliográficos
Autores principales: Li, PeiQi, Lees, Joshua Aaron, Lusk, C. Patrick, Reinisch, Karin M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2020
Materias:
Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7199853/
https://www.ncbi.nlm.nih.gov/pubmed/32182622
http://dx.doi.org/10.1083/jcb.202001161
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author Li, PeiQi
Lees, Joshua Aaron
Lusk, C. Patrick
Reinisch, Karin M.
author_facet Li, PeiQi
Lees, Joshua Aaron
Lusk, C. Patrick
Reinisch, Karin M.
author_sort Li, PeiQi
collection PubMed
description A single particle cryo-EM reconstruction of an ∼160-kD N-terminal fragment of the lipid transport protein VPS13 reveals an ∼160-Å long channel lined with hydrophobic residues suitable for solubilizing multiple lipid fatty acid moieties. The structure suggests that VPS13 and related proteins, like the autophagy protein ATG2, can act as bridges between organelle membranes to allow bulk lipid flow between organelles.
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spelling pubmed-71998532020-11-04 Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes Li, PeiQi Lees, Joshua Aaron Lusk, C. Patrick Reinisch, Karin M. J Cell Biol Report A single particle cryo-EM reconstruction of an ∼160-kD N-terminal fragment of the lipid transport protein VPS13 reveals an ∼160-Å long channel lined with hydrophobic residues suitable for solubilizing multiple lipid fatty acid moieties. The structure suggests that VPS13 and related proteins, like the autophagy protein ATG2, can act as bridges between organelle membranes to allow bulk lipid flow between organelles. Rockefeller University Press 2020-03-17 /pmc/articles/PMC7199853/ /pubmed/32182622 http://dx.doi.org/10.1083/jcb.202001161 Text en © 2020 Li et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Report
Li, PeiQi
Lees, Joshua Aaron
Lusk, C. Patrick
Reinisch, Karin M.
Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes
title Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes
title_full Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes
title_fullStr Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes
title_full_unstemmed Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes
title_short Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes
title_sort cryo-em reconstruction of a vps13 fragment reveals a long groove to channel lipids between membranes
topic Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7199853/
https://www.ncbi.nlm.nih.gov/pubmed/32182622
http://dx.doi.org/10.1083/jcb.202001161
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AT luskcpatrick cryoemreconstructionofavps13fragmentrevealsalonggroovetochannellipidsbetweenmembranes
AT reinischkarinm cryoemreconstructionofavps13fragmentrevealsalonggroovetochannellipidsbetweenmembranes

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