CryoET reveals actin filaments within platelet microtubules

DOI: 10.1038/s41467-024-50424-8

Authors: 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)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 15

State: Published (Approved)
Published: July 2024
Diamond Proposal Number(s): 25452 , 32707

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.

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios III-Titan Krios III at Diamond

Added On: 24/07/2024 11:37

Documents:
s41467-024-50424-8.pdf

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Imaging Tomography Cryo Electron Tomography (Cryo ET)