Nature Communications (Jul 2024)

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

DOI
https://doi.org/10.1038/s41467-024-50424-8
Journal volume & issue
Vol. 15, no. 1
pp. 1 – 8

Abstract

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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.