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ER proteins decipher the tubulin code to regulate organelle distribution
Organelles move along differentially modified microtubules to establish and maintain their proper distributions and functions(1,2). However, how cells interpret these post-translational microtubule modification codes to selectively regulate organelle positioning remains largely unknown. The endoplas...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8732269/ https://www.ncbi.nlm.nih.gov/pubmed/34912111 http://dx.doi.org/10.1038/s41586-021-04204-9 |
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author | Zheng, Pengli Obara, Christopher J. Szczesna, Ewa Nixon-Abell, Jonathon Mahalingan, Kishore K. Roll-Mecak, Antonina Lippincott-Schwartz, Jennifer Blackstone, Craig |
author_facet | Zheng, Pengli Obara, Christopher J. Szczesna, Ewa Nixon-Abell, Jonathon Mahalingan, Kishore K. Roll-Mecak, Antonina Lippincott-Schwartz, Jennifer Blackstone, Craig |
author_sort | Zheng, Pengli |
collection | PubMed |
description | Organelles move along differentially modified microtubules to establish and maintain their proper distributions and functions(1,2). However, how cells interpret these post-translational microtubule modification codes to selectively regulate organelle positioning remains largely unknown. The endoplasmic reticulum (ER) is an interconnected network of diverse morphologies that extends promiscuously throughout the cytoplasm(3), forming abundant contacts with other organelles(4). Dysregulation of endoplasmic reticulum morphology is tightly linked to neurologic disorders and cancer(5,6). Here we demonstrate that three membrane-bound endoplasmic reticulum proteins preferentially interact with different microtubule populations, with CLIMP63 binding centrosome microtubules, kinectin (KTN1) binding perinuclear polyglutamylated microtubules, and p180 binding glutamylated microtubules. Knockout of these proteins or manipulation of microtubule populations and glutamylation status results in marked changes in endoplasmic reticulum positioning, leading to similar redistributions of other organelles. During nutrient starvation, cells modulate CLIMP63 protein levels and p180–microtubule binding to bidirectionally move endoplasmic reticulum and lysosomes for proper autophagic responses. |
format | Online Article Text |
id | pubmed-8732269 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-87322692022-01-18 ER proteins decipher the tubulin code to regulate organelle distribution Zheng, Pengli Obara, Christopher J. Szczesna, Ewa Nixon-Abell, Jonathon Mahalingan, Kishore K. Roll-Mecak, Antonina Lippincott-Schwartz, Jennifer Blackstone, Craig Nature Article Organelles move along differentially modified microtubules to establish and maintain their proper distributions and functions(1,2). However, how cells interpret these post-translational microtubule modification codes to selectively regulate organelle positioning remains largely unknown. The endoplasmic reticulum (ER) is an interconnected network of diverse morphologies that extends promiscuously throughout the cytoplasm(3), forming abundant contacts with other organelles(4). Dysregulation of endoplasmic reticulum morphology is tightly linked to neurologic disorders and cancer(5,6). Here we demonstrate that three membrane-bound endoplasmic reticulum proteins preferentially interact with different microtubule populations, with CLIMP63 binding centrosome microtubules, kinectin (KTN1) binding perinuclear polyglutamylated microtubules, and p180 binding glutamylated microtubules. Knockout of these proteins or manipulation of microtubule populations and glutamylation status results in marked changes in endoplasmic reticulum positioning, leading to similar redistributions of other organelles. During nutrient starvation, cells modulate CLIMP63 protein levels and p180–microtubule binding to bidirectionally move endoplasmic reticulum and lysosomes for proper autophagic responses. Nature Publishing Group UK 2021-12-15 2022 /pmc/articles/PMC8732269/ /pubmed/34912111 http://dx.doi.org/10.1038/s41586-021-04204-9 Text en © The Author(s) 2021, corrected publication 2022 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 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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Zheng, Pengli Obara, Christopher J. Szczesna, Ewa Nixon-Abell, Jonathon Mahalingan, Kishore K. Roll-Mecak, Antonina Lippincott-Schwartz, Jennifer Blackstone, Craig ER proteins decipher the tubulin code to regulate organelle distribution |
title | ER proteins decipher the tubulin code to regulate organelle distribution |
title_full | ER proteins decipher the tubulin code to regulate organelle distribution |
title_fullStr | ER proteins decipher the tubulin code to regulate organelle distribution |
title_full_unstemmed | ER proteins decipher the tubulin code to regulate organelle distribution |
title_short | ER proteins decipher the tubulin code to regulate organelle distribution |
title_sort | er proteins decipher the tubulin code to regulate organelle distribution |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8732269/ https://www.ncbi.nlm.nih.gov/pubmed/34912111 http://dx.doi.org/10.1038/s41586-021-04204-9 |
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