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Updated: Apr 15, 2026

Self-Assembly of Microtubule Tactoids
Published on: June 23, 2022
Buckling behavior of individual and bundled microtubules
Mohammad Soheilypour1, Mohaddeseh Peyro1, Stephen J Peter1
1Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, Berkeley, California.
Abstract:
As the major structural constituent of the cytoskeleton, microtubules (MTs) serve a variety of biological functions that range from facilitating organelle transport to maintaining the mechanical integrity of the cell. Neuronal MTs exhibit a distinct configuration, hexagonally packed bundles of MT filaments, interconnected by MT-associated protein (MAP) tau. Building on our previous work on mechanical response of axonal MT bundles under uniaxial tension, this study is focused on exploring the compression scenarios. Intracellular MTs carry a large fraction of the compressive loads sensed by the cell and therefore, like any other column-like structure, are prone to substantial bending and buckling. Various biological activities, e.g., actomyosin contractility and many pathological conditions are driven or followed by bending, looping, and buckling of MT filaments. The coarse-grained model previously developed in our lab has been used to study the mechanical behavior of individual and bundled in vivo MT filaments under uniaxial compression. Both configurations show tip-localized, decaying, and short-wavelength buckling. This behavior highlights the role of the surrounding cytoplasm and MAP tau on MT buckling behavior, which allows MT filaments to bear much larger compressive forces. It is observed that MAP tau interconnections improve this effect by a factor of two. The enhanced ability of MT bundles to damp buckling waves relative to individual MT filaments, may be interpreted as a self-defense mechanism because it helps axonal MTs to endure harsher environments while maintaining their function. The results indicate that MT filaments in a bundle do not buckle simultaneously implying that the applied stress is not equally shared among the MT filaments, that is a consequence of the nonuniform distribution of MAP tau proteins along the bundle length. Furthermore, from a pathological perspective, it is observed that axonal MT bundles are more vulnerable to failure in compression than tension.
Insights
Microtubules (MTs) in neurons buckle under compression, but MAP tau protein connections significantly enhance their ability to withstand these forces. Bundles are more vulnerable to compression failure than tension.
Area of Science:
- Cellular mechanics
- Biophysics
- Neuroscience
Background:
- Microtubules (MTs) are key cytoskeletal components essential for cell structure and function.
- Neuronal MTs form hexagonally packed bundles stabilized by microtubule-associated protein (MAP) tau.
- Previous research analyzed MT bundle mechanics under tension; this study investigates compression.
Purpose of the Study:
- To explore the compression mechanics of individual and bundled neuronal microtubules (MTs).
- To investigate the role of MAP tau in modulating MT buckling behavior under compressive loads.
- To compare the vulnerability of axonal MT bundles in compression versus tension.
Main Methods:
- Utilized a previously developed coarse-grained model.
- Simulated the mechanical behavior of individual and bundled in vivo MT filaments under uniaxial compression.
Main Results:
- Both individual and bundled MTs exhibit tip-localized, short-wavelength buckling.
- MAP tau interconnections significantly enhance MTs' compressive load-bearing capacity (by a factor of two).
- MT filaments within a bundle do not buckle simultaneously, indicating uneven stress distribution due to nonuniform MAP tau distribution.
Conclusions:
- MAP tau and the surrounding cytoplasm play crucial roles in mitigating MT buckling, allowing MTs to withstand greater compressive forces.
- MT bundles possess enhanced wave-damping capabilities, acting as a protective mechanism for axonal MTs.
- Axonal MT bundles are more susceptible to failure under compression than tension, highlighting potential pathological implications.
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