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Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria
β-Glucocerebrosidase (GCase) mutations lead to glucosylceramide build-up in the lysosome, impacting α-synuclein aggregation and autophagy. Recently, Baden and colleagues found GCase in mitochondria, supporting mitochondrial complex I function and energy metabolism. We believe the newly described rol...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10567851/ https://www.ncbi.nlm.nih.gov/pubmed/37821433 http://dx.doi.org/10.1038/s41467-023-42107-7 |
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author | Klein, Andrés D. Outeiro, Tiago Fleming |
author_facet | Klein, Andrés D. Outeiro, Tiago Fleming |
author_sort | Klein, Andrés D. |
collection | PubMed |
description | β-Glucocerebrosidase (GCase) mutations lead to glucosylceramide build-up in the lysosome, impacting α-synuclein aggregation and autophagy. Recently, Baden and colleagues found GCase in mitochondria, supporting mitochondrial complex I function and energy metabolism. We believe the newly described role of GCase in the mitochondria will inform new Parkinson’s and Gaucher’s disease therapeutics. |
format | Online Article Text |
id | pubmed-10567851 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-105678512023-10-13 Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria Klein, Andrés D. Outeiro, Tiago Fleming Nat Commun Comment β-Glucocerebrosidase (GCase) mutations lead to glucosylceramide build-up in the lysosome, impacting α-synuclein aggregation and autophagy. Recently, Baden and colleagues found GCase in mitochondria, supporting mitochondrial complex I function and energy metabolism. We believe the newly described role of GCase in the mitochondria will inform new Parkinson’s and Gaucher’s disease therapeutics. Nature Publishing Group UK 2023-10-11 /pmc/articles/PMC10567851/ /pubmed/37821433 http://dx.doi.org/10.1038/s41467-023-42107-7 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Comment Klein, Andrés D. Outeiro, Tiago Fleming Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria |
title | Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria |
title_full | Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria |
title_fullStr | Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria |
title_full_unstemmed | Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria |
title_short | Glucocerebrosidase mutations disrupt the lysosome and now the mitochondria |
title_sort | glucocerebrosidase mutations disrupt the lysosome and now the mitochondria |
topic | Comment |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10567851/ https://www.ncbi.nlm.nih.gov/pubmed/37821433 http://dx.doi.org/10.1038/s41467-023-42107-7 |
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