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Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation

Multivesicular endosomes/bodies (MVBs) sort membrane proteins between recycling and degradative pathways. Segregation of membrane proteins onto intraluminal vesicles (ILVs) of MVBs removes them from the recycling pathway and facilitates their degradation following fusion of MVBs with lysosomes. Sort...

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Detalles Bibliográficos
Autores principales: Wong, Louise H., Eden, Emily R., Futter, Clare E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6195632/
https://www.ncbi.nlm.nih.gov/pubmed/30242114
http://dx.doi.org/10.1042/BST20170432
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author Wong, Louise H.
Eden, Emily R.
Futter, Clare E.
author_facet Wong, Louise H.
Eden, Emily R.
Futter, Clare E.
author_sort Wong, Louise H.
collection PubMed
description Multivesicular endosomes/bodies (MVBs) sort membrane proteins between recycling and degradative pathways. Segregation of membrane proteins onto intraluminal vesicles (ILVs) of MVBs removes them from the recycling pathway and facilitates their degradation following fusion of MVBs with lysosomes. Sorting of many cargos onto ILVs depends on the ESCRT (Endosomal Sorting Complex Required for Transport) machinery, although ESCRT-independent mechanisms also exist. In mammalian cells, efficient sorting of ligand-stimulated epidermal growth factor receptors onto ILVs also depends on the tyrosine phosphatase, PTP1B, an ER-localised enzyme that interacts with endosomal targets at membrane contacts between MVBs and the ER. This review focuses on the potential roles played by ER:MVB membrane contact sites in regulating ESCRT-dependent ILV formation.
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spelling pubmed-61956322018-10-30 Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation Wong, Louise H. Eden, Emily R. Futter, Clare E. Biochem Soc Trans Review Articles Multivesicular endosomes/bodies (MVBs) sort membrane proteins between recycling and degradative pathways. Segregation of membrane proteins onto intraluminal vesicles (ILVs) of MVBs removes them from the recycling pathway and facilitates their degradation following fusion of MVBs with lysosomes. Sorting of many cargos onto ILVs depends on the ESCRT (Endosomal Sorting Complex Required for Transport) machinery, although ESCRT-independent mechanisms also exist. In mammalian cells, efficient sorting of ligand-stimulated epidermal growth factor receptors onto ILVs also depends on the tyrosine phosphatase, PTP1B, an ER-localised enzyme that interacts with endosomal targets at membrane contacts between MVBs and the ER. This review focuses on the potential roles played by ER:MVB membrane contact sites in regulating ESCRT-dependent ILV formation. Portland Press Ltd. 2018-10-19 2018-09-21 /pmc/articles/PMC6195632/ /pubmed/30242114 http://dx.doi.org/10.1042/BST20170432 Text en © 2018 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Review Articles
Wong, Louise H.
Eden, Emily R.
Futter, Clare E.
Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation
title Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation
title_full Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation
title_fullStr Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation
title_full_unstemmed Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation
title_short Roles for ER:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation
title_sort roles for er:endosome membrane contact sites in ligand-stimulated intraluminal vesicle formation
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6195632/
https://www.ncbi.nlm.nih.gov/pubmed/30242114
http://dx.doi.org/10.1042/BST20170432
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