Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress
Summary: In yeast, ERMES, which mediates phospholipid transport between the ER and mitochondria, forms a limited number of oligomeric clusters at ER-mitochondria contact sites in a cell. Although the number of the ERMES clusters appears to be regulated to maintain proper inter-organelle phospholipid...
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Elsevier
2022-11-01
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Series: | iScience |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004222016340 |
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author | Yuriko Kakimoto-Takeda Rieko Kojima Hiroya Shiino Manatsu Shinmyo Kazuo Kurokawa Akihiko Nakano Toshiya Endo Yasushi Tamura |
author_facet | Yuriko Kakimoto-Takeda Rieko Kojima Hiroya Shiino Manatsu Shinmyo Kazuo Kurokawa Akihiko Nakano Toshiya Endo Yasushi Tamura |
author_sort | Yuriko Kakimoto-Takeda |
collection | DOAJ |
description | Summary: In yeast, ERMES, which mediates phospholipid transport between the ER and mitochondria, forms a limited number of oligomeric clusters at ER-mitochondria contact sites in a cell. Although the number of the ERMES clusters appears to be regulated to maintain proper inter-organelle phospholipid trafficking, its underlying mechanism and physiological relevance remain poorly understood. Here, we show that mitochondrial dynamics control the number of ERMES clusters. Moreover, we find that ER stress causes dissociation of the ERMES clusters independently of Ire1 and Hac1, canonical ER-stress response pathway components, leading to a delay in the phospholipid transport from the ER to mitochondria. Our biochemical and genetic analyses strongly suggest that the impaired phospholipid transport contributes to phospholipid accumulation in the ER, expanding the ER for ER stress attenuation. We thus propose that the ERMES dissociation constitutes an overlooked pathway of the ER stress response that operates in addition to the canonical Ire1/Hac1-dependent pathway. |
first_indexed | 2024-04-12T15:18:58Z |
format | Article |
id | doaj.art-e1aba48a5485490da62f70182a6e4bc2 |
institution | Directory Open Access Journal |
issn | 2589-0042 |
language | English |
last_indexed | 2024-04-12T15:18:58Z |
publishDate | 2022-11-01 |
publisher | Elsevier |
record_format | Article |
series | iScience |
spelling | doaj.art-e1aba48a5485490da62f70182a6e4bc22022-12-22T03:27:33ZengElsevieriScience2589-00422022-11-012511105362Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stressYuriko Kakimoto-Takeda0Rieko Kojima1Hiroya Shiino2Manatsu Shinmyo3Kazuo Kurokawa4Akihiko Nakano5Toshiya Endo6Yasushi Tamura7Department of Biochemistry and Molecular Biology, Graduate School of Medical Science, Yamagata University, 2-2-2 Iidanishi, Yamagata 990-9585, JapanFaculty of Science, Yamagata University, 1-4-12 Kojirakawa-machi, Yamagata 990-8560, JapanFaculty of Science, Yamagata University, 1-4-12 Kojirakawa-machi, Yamagata 990-8560, JapanFaculty of Science, Yamagata University, 1-4-12 Kojirakawa-machi, Yamagata 990-8560, JapanLive Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama 351-0198, JapanLive Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama 351-0198, JapanFaculty of Life Sciences, Kyoto Sangyo University, Kamigamo-motoyama, Kita-ku, Kyoto 603-8555, Japan; Institute for Protein Dynamics, Kyoto Sangyo University, Kamigamo-motoyama, Kita-ku, Kyoto 603-8555, JapanFaculty of Science, Yamagata University, 1-4-12 Kojirakawa-machi, Yamagata 990-8560, Japan; Corresponding authorSummary: In yeast, ERMES, which mediates phospholipid transport between the ER and mitochondria, forms a limited number of oligomeric clusters at ER-mitochondria contact sites in a cell. Although the number of the ERMES clusters appears to be regulated to maintain proper inter-organelle phospholipid trafficking, its underlying mechanism and physiological relevance remain poorly understood. Here, we show that mitochondrial dynamics control the number of ERMES clusters. Moreover, we find that ER stress causes dissociation of the ERMES clusters independently of Ire1 and Hac1, canonical ER-stress response pathway components, leading to a delay in the phospholipid transport from the ER to mitochondria. Our biochemical and genetic analyses strongly suggest that the impaired phospholipid transport contributes to phospholipid accumulation in the ER, expanding the ER for ER stress attenuation. We thus propose that the ERMES dissociation constitutes an overlooked pathway of the ER stress response that operates in addition to the canonical Ire1/Hac1-dependent pathway.http://www.sciencedirect.com/science/article/pii/S2589004222016340Biological sciencesCell biologyFunctional aspects of cell biology |
spellingShingle | Yuriko Kakimoto-Takeda Rieko Kojima Hiroya Shiino Manatsu Shinmyo Kazuo Kurokawa Akihiko Nakano Toshiya Endo Yasushi Tamura Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress iScience Biological sciences Cell biology Functional aspects of cell biology |
title | Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress |
title_full | Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress |
title_fullStr | Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress |
title_full_unstemmed | Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress |
title_short | Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress |
title_sort | dissociation of ermes clusters plays a key role in attenuating the endoplasmic reticulum stress |
topic | Biological sciences Cell biology Functional aspects of cell biology |
url | http://www.sciencedirect.com/science/article/pii/S2589004222016340 |
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