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PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria
Endosomes are compositionally dynamic organelles that regulate signaling, nutrient status and organelle quality by specifying whether material entering the cells will be shuttled back to the cell surface or degraded by the lysosome. Recently, membrane contact sites (MCSs) between the endoplasmic ret...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7371716/ https://www.ncbi.nlm.nih.gov/pubmed/32686675 http://dx.doi.org/10.1038/s41467-020-17451-7 |
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author | Elbaz-Alon, Yael Guo, Yuting Segev, Nadav Harel, Michal Quinnell, Daniel E. Geiger, Tamar Avinoam, Ori Li, Dong Nunnari, Jodi |
author_facet | Elbaz-Alon, Yael Guo, Yuting Segev, Nadav Harel, Michal Quinnell, Daniel E. Geiger, Tamar Avinoam, Ori Li, Dong Nunnari, Jodi |
author_sort | Elbaz-Alon, Yael |
collection | PubMed |
description | Endosomes are compositionally dynamic organelles that regulate signaling, nutrient status and organelle quality by specifying whether material entering the cells will be shuttled back to the cell surface or degraded by the lysosome. Recently, membrane contact sites (MCSs) between the endoplasmic reticulum (ER) and endosomes have emerged as important players in endosomal protein sorting, dynamics and motility. Here, we show that PDZD8, a Synaptotagmin-like Mitochondrial lipid-binding Proteins (SMP) domain-containing ER transmembrane protein, utilizes distinct domains to interact with Rab7-GTP and the ER transmembrane protein Protrudin and together these components localize to an ER-late endosome MCS. At these ER-late endosome MCSs, mitochondria are also recruited to form a three-way contact. Thus, our data indicate that PDZD8 is a shared component of two distinct MCSs and suggest a role for SMP-mediated lipid transport in the regulation of endosome function. |
format | Online Article Text |
id | pubmed-7371716 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73717162020-07-22 PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria Elbaz-Alon, Yael Guo, Yuting Segev, Nadav Harel, Michal Quinnell, Daniel E. Geiger, Tamar Avinoam, Ori Li, Dong Nunnari, Jodi Nat Commun Article Endosomes are compositionally dynamic organelles that regulate signaling, nutrient status and organelle quality by specifying whether material entering the cells will be shuttled back to the cell surface or degraded by the lysosome. Recently, membrane contact sites (MCSs) between the endoplasmic reticulum (ER) and endosomes have emerged as important players in endosomal protein sorting, dynamics and motility. Here, we show that PDZD8, a Synaptotagmin-like Mitochondrial lipid-binding Proteins (SMP) domain-containing ER transmembrane protein, utilizes distinct domains to interact with Rab7-GTP and the ER transmembrane protein Protrudin and together these components localize to an ER-late endosome MCS. At these ER-late endosome MCSs, mitochondria are also recruited to form a three-way contact. Thus, our data indicate that PDZD8 is a shared component of two distinct MCSs and suggest a role for SMP-mediated lipid transport in the regulation of endosome function. Nature Publishing Group UK 2020-07-20 /pmc/articles/PMC7371716/ /pubmed/32686675 http://dx.doi.org/10.1038/s41467-020-17451-7 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Elbaz-Alon, Yael Guo, Yuting Segev, Nadav Harel, Michal Quinnell, Daniel E. Geiger, Tamar Avinoam, Ori Li, Dong Nunnari, Jodi PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria |
title | PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria |
title_full | PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria |
title_fullStr | PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria |
title_full_unstemmed | PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria |
title_short | PDZD8 interacts with Protrudin and Rab7 at ER-late endosome membrane contact sites associated with mitochondria |
title_sort | pdzd8 interacts with protrudin and rab7 at er-late endosome membrane contact sites associated with mitochondria |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7371716/ https://www.ncbi.nlm.nih.gov/pubmed/32686675 http://dx.doi.org/10.1038/s41467-020-17451-7 |
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