CryoET reveals actin filaments within platelet microtubules
Abstract Crosstalk between the actin and microtubule cytoskeletons is important for many cellular processes. Recent studies have shown that microtubules and F-actin can assemble to form a composite structure where F-actin occupies the microtubule lumen. Whether these cytoskeletal hybrids exist in ph...
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| Format: | Article |
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Nature Portfolio
2024-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-50424-8 |
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| _version_ | 1846147687722778624 |
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| author | Chisato Tsuji Marston Bradshaw Megan F. Allen Molly L. Jackson Judith Mantell Ufuk Borucu Alastair W. Poole Paul Verkade Ingeborg Hers Danielle M. Paul Mark P. Dodding |
| author_facet | Chisato Tsuji Marston Bradshaw Megan F. Allen Molly L. Jackson Judith Mantell Ufuk Borucu Alastair W. Poole Paul Verkade Ingeborg Hers Danielle M. Paul Mark P. Dodding |
| author_sort | Chisato Tsuji |
| collection | DOAJ |
| description | Abstract Crosstalk between the actin and microtubule cytoskeletons is important for many cellular processes. Recent studies have shown that microtubules and F-actin can assemble to form a composite structure where F-actin occupies the microtubule lumen. Whether these cytoskeletal hybrids exist in physiological settings and how they are formed is unclear. Here, we show that the short-crossover Class I actin filament previously identified inside microtubules in human HAP1 cells is cofilin-bound F-actin. Lumenal F-actin can be reconstituted in vitro, but cofilin is not essential. Moreover, actin filaments with both cofilin-bound and canonical morphologies reside within human platelet microtubules under physiological conditions. We propose that stress placed upon the microtubule network during motor-driven microtubule looping and sliding may facilitate the incorporation of actin into microtubules. |
| format | Article |
| id | doaj-art-9f1e9987006d4254bcc55c15f45b131c |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2024-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-9f1e9987006d4254bcc55c15f45b131c2024-12-01T12:34:09ZengNature PortfolioNature Communications2041-17232024-07-011511810.1038/s41467-024-50424-8CryoET reveals actin filaments within platelet microtubulesChisato Tsuji0Marston Bradshaw1Megan F. Allen2Molly L. Jackson3Judith Mantell4Ufuk Borucu5Alastair W. Poole6Paul Verkade7Ingeborg Hers8Danielle M. Paul9Mark P. Dodding10School of Biochemistry, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Physiology, Pharmacology and Neuroscience, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Physiology, Pharmacology and Neuroscience, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Physiology, Pharmacology and Neuroscience, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Biochemistry, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolGW4 Facility for High-Resolution Electron Cryo-Microscopy, University of BristolSchool of Physiology, Pharmacology and Neuroscience, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Biochemistry, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Physiology, Pharmacology and Neuroscience, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Physiology, Pharmacology and Neuroscience, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolSchool of Biochemistry, Faculty of Health and Life Sciences, Biomedical Sciences Building, University Walk, University of BristolAbstract Crosstalk between the actin and microtubule cytoskeletons is important for many cellular processes. Recent studies have shown that microtubules and F-actin can assemble to form a composite structure where F-actin occupies the microtubule lumen. Whether these cytoskeletal hybrids exist in physiological settings and how they are formed is unclear. Here, we show that the short-crossover Class I actin filament previously identified inside microtubules in human HAP1 cells is cofilin-bound F-actin. Lumenal F-actin can be reconstituted in vitro, but cofilin is not essential. Moreover, actin filaments with both cofilin-bound and canonical morphologies reside within human platelet microtubules under physiological conditions. We propose that stress placed upon the microtubule network during motor-driven microtubule looping and sliding may facilitate the incorporation of actin into microtubules.https://doi.org/10.1038/s41467-024-50424-8 |
| spellingShingle | Chisato Tsuji Marston Bradshaw Megan F. Allen Molly L. Jackson Judith Mantell Ufuk Borucu Alastair W. Poole Paul Verkade Ingeborg Hers Danielle M. Paul Mark P. Dodding CryoET reveals actin filaments within platelet microtubules Nature Communications |
| title | CryoET reveals actin filaments within platelet microtubules |
| title_full | CryoET reveals actin filaments within platelet microtubules |
| title_fullStr | CryoET reveals actin filaments within platelet microtubules |
| title_full_unstemmed | CryoET reveals actin filaments within platelet microtubules |
| title_short | CryoET reveals actin filaments within platelet microtubules |
| title_sort | cryoet reveals actin filaments within platelet microtubules |
| url | https://doi.org/10.1038/s41467-024-50424-8 |
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