The rate of microtubule breaking increases exponentially with curvature

• Published in: Scientific reports Vol. 12; no. 1; p. 20899
• Main Authors: Tsitkov, Stanislav, Rodriguez, 3rd, Juan B, Bassir Kazeruni, Neda M, Sweet, May, Nitta, Takahiro, Hess, Henry
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 03.12.2022; Nature Publishing Group UK; Nature Portfolio
• Subjects: Cell Migration Assays; Cytoskeleton; Enzymes; Gliding; Kinesin; Kinesins; Membrane Proteins; Microscopy; Microtubules; Paclitaxel; Proteins; Science & Technology - Other Topics; Tensile strength; Tubulin
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-022-24912-0

Microtubules, cylindrical assemblies of tubulin proteins with a 25 nm diameter and micrometer lengths, are a central part of the cytoskeleton and also serve as building blocks for nanobiodevices. Microtubule breaking can result from the activity of severing enzymes and mechanical stress. Breaking can lead to a loss of structural integrity, or an increase in the numbers of microtubules. We observed breaking of taxol-stabilized microtubules in a gliding motility assay where microtubules are propelled by surface-adhered kinesin-1 motor proteins. We find that over 95% of all breaking events are associated with the strong bending following pinning events (where the leading tip of the microtubule becomes stuck). Furthermore, the breaking rate increased exponentially with increasing curvature. These observations are explained by a model accounting for the complex mechanochemistry of a microtubule. The presence of severing enzymes is not required to observe breaking at rates comparable to those measured previously in cells.