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Instruments / Technical Area	Publication Details	Published	Actions
Krios III-Titan Krios III at Diamond	CryoET reveals actin filaments within platelet microtubules 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 Nature Communications 15 DOI: 10.1038/s41467-024-50424-8 Diamond Proposal Number(s): [25452, 32707] Open Access Show Abstract ▼ 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.	Jul 2024
Krios I-Titan Krios I at Diamond	Zebrafish as a model for cardiac disease; Cryo-EM structure of native cardiac thin filaments from Danio Rerio Marston Bradshaw , John M. Squire , Edward Morris , Georgia Atkinson , Rebecca Richardson , Jon Lees , Massimo Caputo , Giulia M. Bigotti , Danielle M. Paul Journal Of Muscle Research And Cell Motility 7 DOI: 10.1007/s10974-023-09653-5 Diamond Proposal Number(s): [32707] Open Access Show Abstract ▼ Abstract: Actin, tropomyosin and troponin, the proteins that comprise the contractile apparatus of the cardiac thin filament, are highly conserved across species. We have used cryo-EM to study the three-dimensional structure of the zebrafish cardiac thin and actin filaments. With 70% of human genes having an obvious zebrafish orthologue, and conservation of 85% of disease-causing genes, zebrafish are a good animal model for the study of human disease. Our structure of the zebrafish thin filament reveals the molecular interactions between the constituent proteins, showing that the fundamental organisation of the complex is the same as that reported in the human reconstituted thin filament. A reconstruction of zebrafish cardiac F-actin demonstrates no deviations from human cardiac actin over an extended length of 14 actin subunits. Modelling zebrafish homology models into our maps enabled us to compare, in detail, the similarity with human models. The structural similarities of troponin-T in particular, a region known to contain a hypertrophic cardiomyopathy ‘hotspot’, confirm the suitability of zebrafish to study these disease-causing mutations.	Jul 2023

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