HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response
The mitochondrial unfolded protein response (UPRmt) is characterized by the transcriptional induction of mitochondrial chaperone and protease genes in response to impaired mitochondrial proteostasis and is regulated by ATF5 and CHOP in mammalian cells. However, the detailed mechanisms underlying the...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2020-06-01
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| Series: | FEBS Open Bio |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/2211-5463.12863 |
| _version_ | 1819194730694574080 |
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| author | Arpit Katiyar Mitsuaki Fujimoto Ke Tan Ai Kurashima Pratibha Srivastava Mariko Okada Ryosuke Takii Akira Nakai |
| author_facet | Arpit Katiyar Mitsuaki Fujimoto Ke Tan Ai Kurashima Pratibha Srivastava Mariko Okada Ryosuke Takii Akira Nakai |
| author_sort | Arpit Katiyar |
| collection | DOAJ |
| description | The mitochondrial unfolded protein response (UPRmt) is characterized by the transcriptional induction of mitochondrial chaperone and protease genes in response to impaired mitochondrial proteostasis and is regulated by ATF5 and CHOP in mammalian cells. However, the detailed mechanisms underlying the UPRmt are currently unclear. Here, we show that HSF1 is required for activation of mitochondrial chaperone genes, including HSP60, HSP10, and mtHSP70, in mouse embryonic fibroblasts during inhibition of matrix chaperone TRAP1, protease Lon, or electron transfer complex 1 activity. HSF1 bound constitutively to mitochondrial chaperone gene promoters, and we observed that its occupancy was remarkably enhanced at different levels during the UPRmt. Furthermore, HSF1 supported the maintenance of mitochondrial function under the same conditions. These results demonstrate that HSF1 is required for induction of mitochondrial chaperones during the UPRmt, and thus, it may be one of the guardians of mitochondrial function under conditions of impaired mitochondrial proteostasis. |
| first_indexed | 2024-12-23T02:01:31Z |
| format | Article |
| id | doaj.art-ed47cad0ab0a4a8099f07a67a712671f |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-12-23T02:01:31Z |
| publishDate | 2020-06-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-ed47cad0ab0a4a8099f07a67a712671f2022-12-21T18:03:59ZengWileyFEBS Open Bio2211-54632020-06-011061135114810.1002/2211-5463.12863HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein responseArpit Katiyar0Mitsuaki Fujimoto1Ke Tan2Ai Kurashima3Pratibha Srivastava4Mariko Okada5Ryosuke Takii6Akira Nakai7Department of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanDepartment of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanDepartment of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanDepartment of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanDepartment of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanDepartment of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanDepartment of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanDepartment of Biochemistry and Molecular Biology Yamaguchi University School of Medicine Ube JapanThe mitochondrial unfolded protein response (UPRmt) is characterized by the transcriptional induction of mitochondrial chaperone and protease genes in response to impaired mitochondrial proteostasis and is regulated by ATF5 and CHOP in mammalian cells. However, the detailed mechanisms underlying the UPRmt are currently unclear. Here, we show that HSF1 is required for activation of mitochondrial chaperone genes, including HSP60, HSP10, and mtHSP70, in mouse embryonic fibroblasts during inhibition of matrix chaperone TRAP1, protease Lon, or electron transfer complex 1 activity. HSF1 bound constitutively to mitochondrial chaperone gene promoters, and we observed that its occupancy was remarkably enhanced at different levels during the UPRmt. Furthermore, HSF1 supported the maintenance of mitochondrial function under the same conditions. These results demonstrate that HSF1 is required for induction of mitochondrial chaperones during the UPRmt, and thus, it may be one of the guardians of mitochondrial function under conditions of impaired mitochondrial proteostasis.https://doi.org/10.1002/2211-5463.12863heat shock proteinHSF1mitochondriaproteostasisproteotoxic stressSSBP1 |
| spellingShingle | Arpit Katiyar Mitsuaki Fujimoto Ke Tan Ai Kurashima Pratibha Srivastava Mariko Okada Ryosuke Takii Akira Nakai HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response FEBS Open Bio heat shock protein HSF1 mitochondria proteostasis proteotoxic stress SSBP1 |
| title | HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response |
| title_full | HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response |
| title_fullStr | HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response |
| title_full_unstemmed | HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response |
| title_short | HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response |
| title_sort | hsf1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response |
| topic | heat shock protein HSF1 mitochondria proteostasis proteotoxic stress SSBP1 |
| url | https://doi.org/10.1002/2211-5463.12863 |
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