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 () and Mark P. Dodding ()
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Chisato Tsuji: University of Bristol
Marston Bradshaw: University of Bristol
Megan F. Allen: University of Bristol
Molly L. Jackson: University of Bristol
Judith Mantell: University of Bristol
Ufuk Borucu: University of Bristol
Alastair W. Poole: University of Bristol
Paul Verkade: University of Bristol
Ingeborg Hers: University of Bristol
Danielle M. Paul: University of Bristol
Mark P. Dodding: University of Bristol

Nature Communications, 2024, vol. 15, issue 1, 1-8

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.

Date: 2024
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DOI: 10.1038/s41467-024-50424-8

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