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LC3-associated endocytosis and the functions of Rubicon and ATG16L1
LC3-associated endocytosis (LANDO) is a noncanonical function of the autophagy machinery, in which LC3 (microtubule-associated protein light chain) is conjugated to rab5-positive endosomes, using a portion of the canonical autophagy pathway. LANDO was initially discovered in a murine model of Alzhei...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604520/ https://www.ncbi.nlm.nih.gov/pubmed/36288306 http://dx.doi.org/10.1126/sciadv.abo5600 |
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author | Magné, Joëlle Green, Douglas R. |
author_facet | Magné, Joëlle Green, Douglas R. |
author_sort | Magné, Joëlle |
collection | PubMed |
description | LC3-associated endocytosis (LANDO) is a noncanonical function of the autophagy machinery, in which LC3 (microtubule-associated protein light chain) is conjugated to rab5-positive endosomes, using a portion of the canonical autophagy pathway. LANDO was initially discovered in a murine model of Alzheimer’s disease as a critical regulator of amyloid-β receptor recycling in microglial cells, playing a protective role against neuronal loss and memory impairment. Recent evidence suggests an emerging role of LANDO in cytokine receptor signaling and innate immunity. Here, we discuss the regulation of two crucial effectors of LANDO, Rubicon and ATG16L1, and their impact on endocytosis, autophagy, and phagocytosis. |
format | Online Article Text |
id | pubmed-9604520 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-96045202022-11-04 LC3-associated endocytosis and the functions of Rubicon and ATG16L1 Magné, Joëlle Green, Douglas R. Sci Adv Biomedicine and Life Sciences LC3-associated endocytosis (LANDO) is a noncanonical function of the autophagy machinery, in which LC3 (microtubule-associated protein light chain) is conjugated to rab5-positive endosomes, using a portion of the canonical autophagy pathway. LANDO was initially discovered in a murine model of Alzheimer’s disease as a critical regulator of amyloid-β receptor recycling in microglial cells, playing a protective role against neuronal loss and memory impairment. Recent evidence suggests an emerging role of LANDO in cytokine receptor signaling and innate immunity. Here, we discuss the regulation of two crucial effectors of LANDO, Rubicon and ATG16L1, and their impact on endocytosis, autophagy, and phagocytosis. American Association for the Advancement of Science 2022-10-26 /pmc/articles/PMC9604520/ /pubmed/36288306 http://dx.doi.org/10.1126/sciadv.abo5600 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Magné, Joëlle Green, Douglas R. LC3-associated endocytosis and the functions of Rubicon and ATG16L1 |
title | LC3-associated endocytosis and the functions of Rubicon and ATG16L1 |
title_full | LC3-associated endocytosis and the functions of Rubicon and ATG16L1 |
title_fullStr | LC3-associated endocytosis and the functions of Rubicon and ATG16L1 |
title_full_unstemmed | LC3-associated endocytosis and the functions of Rubicon and ATG16L1 |
title_short | LC3-associated endocytosis and the functions of Rubicon and ATG16L1 |
title_sort | lc3-associated endocytosis and the functions of rubicon and atg16l1 |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9604520/ https://www.ncbi.nlm.nih.gov/pubmed/36288306 http://dx.doi.org/10.1126/sciadv.abo5600 |
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