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An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease
Over the last decades, research on the pathobiology of neurodegenerative diseases has greatly evolved, revealing potential targets and mechanisms linked to their pathogenesis. Parkinson’s disease (PD) is no exception, and recent studies point to the involvement of endolysosomal defects in PD. The en...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10669493/ https://www.ncbi.nlm.nih.gov/pubmed/38002327 http://dx.doi.org/10.3390/biom13111645 |
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author | Komori, Tadayuki Kuwahara, Tomoki |
author_facet | Komori, Tadayuki Kuwahara, Tomoki |
author_sort | Komori, Tadayuki |
collection | PubMed |
description | Over the last decades, research on the pathobiology of neurodegenerative diseases has greatly evolved, revealing potential targets and mechanisms linked to their pathogenesis. Parkinson’s disease (PD) is no exception, and recent studies point to the involvement of endolysosomal defects in PD. The endolysosomal system, which tightly controls a flow of endocytosed vesicles targeted either for degradation or recycling, is regulated by a number of Rab GTPases. Their associations with leucine-rich repeat kinase 2 (LRRK2), a major causative and risk protein of PD, has also been one of the hot topics in the field. Understanding their interactions and functions is critical for unraveling their contribution to PD pathogenesis. In this review, we summarize recent studies on LRRK2 and Rab GTPases and attempt to provide more insight into the interaction of LRRK2 with each Rab and its relationship to PD. |
format | Online Article Text |
id | pubmed-10669493 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106694932023-11-13 An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease Komori, Tadayuki Kuwahara, Tomoki Biomolecules Review Over the last decades, research on the pathobiology of neurodegenerative diseases has greatly evolved, revealing potential targets and mechanisms linked to their pathogenesis. Parkinson’s disease (PD) is no exception, and recent studies point to the involvement of endolysosomal defects in PD. The endolysosomal system, which tightly controls a flow of endocytosed vesicles targeted either for degradation or recycling, is regulated by a number of Rab GTPases. Their associations with leucine-rich repeat kinase 2 (LRRK2), a major causative and risk protein of PD, has also been one of the hot topics in the field. Understanding their interactions and functions is critical for unraveling their contribution to PD pathogenesis. In this review, we summarize recent studies on LRRK2 and Rab GTPases and attempt to provide more insight into the interaction of LRRK2 with each Rab and its relationship to PD. MDPI 2023-11-13 /pmc/articles/PMC10669493/ /pubmed/38002327 http://dx.doi.org/10.3390/biom13111645 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Komori, Tadayuki Kuwahara, Tomoki An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease |
title | An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease |
title_full | An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease |
title_fullStr | An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease |
title_full_unstemmed | An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease |
title_short | An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease |
title_sort | update on the interplay between lrrk2, rab gtpases and parkinson’s disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10669493/ https://www.ncbi.nlm.nih.gov/pubmed/38002327 http://dx.doi.org/10.3390/biom13111645 |
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