Ferroptosis-protective membrane domains in quiescence
Summary: Quiescence is a common cellular state, required for stem cell maintenance and microorganismal survival under stress conditions or starvation. However, the mechanisms promoting quiescence maintenance remain poorly known. Plasma membrane components segregate into distinct microdomains, yet th...
| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-12-01
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| Series: | Cell Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124723015735 |
| _version_ | 1797391810798026752 |
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| author | Amalia H. Megarioti Bianca M. Esch Alexandros Athanasopoulos Dimitrios Koulouris Manousos Makridakis Vasiliki Lygirou Martina Samiotaki Jerome Zoidakis Vicky Sophianopoulou Bruno André Florian Fröhlich Christos Gournas |
| author_facet | Amalia H. Megarioti Bianca M. Esch Alexandros Athanasopoulos Dimitrios Koulouris Manousos Makridakis Vasiliki Lygirou Martina Samiotaki Jerome Zoidakis Vicky Sophianopoulou Bruno André Florian Fröhlich Christos Gournas |
| author_sort | Amalia H. Megarioti |
| collection | DOAJ |
| description | Summary: Quiescence is a common cellular state, required for stem cell maintenance and microorganismal survival under stress conditions or starvation. However, the mechanisms promoting quiescence maintenance remain poorly known. Plasma membrane components segregate into distinct microdomains, yet the role of this compartmentalization in quiescence remains unexplored. Here, we show that flavodoxin-like proteins (FLPs), ubiquinone reductases of the yeast eisosome membrane compartment, protect quiescent cells from lipid peroxidation and ferroptosis. Eisosomes and FLPs expand specifically in respiratory-active quiescent cells, and mutants lacking either show accelerated aging and defective quiescence maintenance and accumulate peroxidized phospholipids with monounsaturated or polyunsaturated fatty acids (PUFAs). FLPs are essential for the extramitochondrial regeneration of the lipophilic antioxidant ubiquinol. FLPs, alongside the Gpx1/2/3 glutathione peroxidases, prevent iron-driven, PUFA-dependent ferroptotic cell death. Our work describes ferroptosis-protective mechanisms in yeast and introduces plasma membrane compartmentalization as an important factor in the long-term survival of quiescent cells. |
| first_indexed | 2024-03-08T23:38:06Z |
| format | Article |
| id | doaj.art-c27731d6dfd14f67987fe4b07a4b64c7 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-03-08T23:38:06Z |
| publishDate | 2023-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-c27731d6dfd14f67987fe4b07a4b64c72023-12-14T05:22:44ZengElsevierCell Reports2211-12472023-12-014212113561Ferroptosis-protective membrane domains in quiescenceAmalia H. Megarioti0Bianca M. Esch1Alexandros Athanasopoulos2Dimitrios Koulouris3Manousos Makridakis4Vasiliki Lygirou5Martina Samiotaki6Jerome Zoidakis7Vicky Sophianopoulou8Bruno André9Florian Fröhlich10Christos Gournas11Microbial Molecular Genetics Laboratory, Institute of Biosciences and Applications, National Center for Scientific Research ''Demokritos,” 15341 Agia Paraskevi, Greece; Department of Biology, National and Kapodistrian University of Athens, Panepistimioupolis, 15784 Athens, GreeceBioanalytical Chemistry Section, Department of Biology/Chemistry, Osnabrück University, 49076 Osnabrück, GermanyMicrobial Molecular Genetics Laboratory, Institute of Biosciences and Applications, National Center for Scientific Research ''Demokritos,” 15341 Agia Paraskevi, GreeceMicrobial Molecular Genetics Laboratory, Institute of Biosciences and Applications, National Center for Scientific Research ''Demokritos,” 15341 Agia Paraskevi, GreeceBiotechnology Division, Systems Biology Center, Biomedical Research Foundation of the Academy of Athens, 11527 Athens, GreeceBiotechnology Division, Systems Biology Center, Biomedical Research Foundation of the Academy of Athens, 11527 Athens, GreeceInstitute for Bioinnovation, Biomedical Sciences Research Center “Alexander Fleming,” 16672 Vari, GreeceDepartment of Biology, National and Kapodistrian University of Athens, Panepistimioupolis, 15784 Athens, Greece; Biotechnology Division, Systems Biology Center, Biomedical Research Foundation of the Academy of Athens, 11527 Athens, GreeceMicrobial Molecular Genetics Laboratory, Institute of Biosciences and Applications, National Center for Scientific Research ''Demokritos,” 15341 Agia Paraskevi, GreeceMolecular Physiology of the Cell Laboratory, Université Libre de Bruxelles (ULB), IBMM, 6041 Gosselies, BelgiumBioanalytical Chemistry Section, Department of Biology/Chemistry, Osnabrück University, 49076 Osnabrück, Germany; Center for Cellular Nanoanalytic Osnabrück (CellNanOs), Osnabrück University, 49076 Osnabrück, Germany; Corresponding authorMicrobial Molecular Genetics Laboratory, Institute of Biosciences and Applications, National Center for Scientific Research ''Demokritos,” 15341 Agia Paraskevi, Greece; Corresponding authorSummary: Quiescence is a common cellular state, required for stem cell maintenance and microorganismal survival under stress conditions or starvation. However, the mechanisms promoting quiescence maintenance remain poorly known. Plasma membrane components segregate into distinct microdomains, yet the role of this compartmentalization in quiescence remains unexplored. Here, we show that flavodoxin-like proteins (FLPs), ubiquinone reductases of the yeast eisosome membrane compartment, protect quiescent cells from lipid peroxidation and ferroptosis. Eisosomes and FLPs expand specifically in respiratory-active quiescent cells, and mutants lacking either show accelerated aging and defective quiescence maintenance and accumulate peroxidized phospholipids with monounsaturated or polyunsaturated fatty acids (PUFAs). FLPs are essential for the extramitochondrial regeneration of the lipophilic antioxidant ubiquinol. FLPs, alongside the Gpx1/2/3 glutathione peroxidases, prevent iron-driven, PUFA-dependent ferroptotic cell death. Our work describes ferroptosis-protective mechanisms in yeast and introduces plasma membrane compartmentalization as an important factor in the long-term survival of quiescent cells.http://www.sciencedirect.com/science/article/pii/S2211124723015735CP: Cell biology |
| spellingShingle | Amalia H. Megarioti Bianca M. Esch Alexandros Athanasopoulos Dimitrios Koulouris Manousos Makridakis Vasiliki Lygirou Martina Samiotaki Jerome Zoidakis Vicky Sophianopoulou Bruno André Florian Fröhlich Christos Gournas Ferroptosis-protective membrane domains in quiescence Cell Reports CP: Cell biology |
| title | Ferroptosis-protective membrane domains in quiescence |
| title_full | Ferroptosis-protective membrane domains in quiescence |
| title_fullStr | Ferroptosis-protective membrane domains in quiescence |
| title_full_unstemmed | Ferroptosis-protective membrane domains in quiescence |
| title_short | Ferroptosis-protective membrane domains in quiescence |
| title_sort | ferroptosis protective membrane domains in quiescence |
| topic | CP: Cell biology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124723015735 |
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