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The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites
The conserved VPS13 proteins constitute a new family of lipid transporters at membrane contact sites. These large proteins are suspected to bridge membranes and form a direct channel for lipid transport between organelles. Mutations in the 4 human homologs (VPS13A–D) are associated with a number of...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7999203/ https://www.ncbi.nlm.nih.gov/pubmed/33809364 http://dx.doi.org/10.3390/ijms22062905 |
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author | Dziurdzik, Samantha Katarzyna Conibear, Elizabeth |
author_facet | Dziurdzik, Samantha Katarzyna Conibear, Elizabeth |
author_sort | Dziurdzik, Samantha Katarzyna |
collection | PubMed |
description | The conserved VPS13 proteins constitute a new family of lipid transporters at membrane contact sites. These large proteins are suspected to bridge membranes and form a direct channel for lipid transport between organelles. Mutations in the 4 human homologs (VPS13A–D) are associated with a number of neurological disorders, but little is known about their precise functions or the relevant contact sites affected in disease. In contrast, yeast has a single Vps13 protein which is recruited to multiple organelles and contact sites. The yeast model system has proved useful for studying the function of Vps13 at different organelles and identifying the localization determinants responsible for its membrane targeting. In this review we describe recent advances in our understanding of VPS13 proteins with a focus on yeast research. |
format | Online Article Text |
id | pubmed-7999203 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79992032021-03-28 The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites Dziurdzik, Samantha Katarzyna Conibear, Elizabeth Int J Mol Sci Review The conserved VPS13 proteins constitute a new family of lipid transporters at membrane contact sites. These large proteins are suspected to bridge membranes and form a direct channel for lipid transport between organelles. Mutations in the 4 human homologs (VPS13A–D) are associated with a number of neurological disorders, but little is known about their precise functions or the relevant contact sites affected in disease. In contrast, yeast has a single Vps13 protein which is recruited to multiple organelles and contact sites. The yeast model system has proved useful for studying the function of Vps13 at different organelles and identifying the localization determinants responsible for its membrane targeting. In this review we describe recent advances in our understanding of VPS13 proteins with a focus on yeast research. MDPI 2021-03-12 /pmc/articles/PMC7999203/ /pubmed/33809364 http://dx.doi.org/10.3390/ijms22062905 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Dziurdzik, Samantha Katarzyna Conibear, Elizabeth The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites |
title | The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites |
title_full | The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites |
title_fullStr | The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites |
title_full_unstemmed | The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites |
title_short | The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites |
title_sort | vps13 family of lipid transporters and its role at membrane contact sites |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7999203/ https://www.ncbi.nlm.nih.gov/pubmed/33809364 http://dx.doi.org/10.3390/ijms22062905 |
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