Characterization of microtubule buckling in living cells

Pallavicini, Carla; Monastra, Alejandro; Bardeci, Nicolás Diego González; Wetzler, Diana E.; Levi, Valeria; Bruno, Luciana

doi:10.1007/s00249-017-1207-9

Cited by 12 publications

(9 citation statements)

References 42 publications

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“…In addition to the overall increased microtubule alignment and very distinct radial organization, we observe an influence of the vimentin IF network, which surrounds the microtubules as a viscoelastic matrix, on the microtubule bending. The order of magnitude of our measured curvature values is nicely in line with previous literature on microtubule shapes in cells 21,30,31 . The effect of the vimentin IF network becomes visible when analyzing the microtubule bending in a spatially resolved manner.…”

Section: Discussionsupporting

confidence: 91%

Vimentin intermediate filaments structure and mechanically support microtubules in cells

Blob

Ventzke

Nies

et al. 2023

Preprint

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The eukaryotic cytoskeleton comprises three types of mechanically distinct biopoly-mers – actin filaments, microtubules and intermediate filaments (IFs)– along with pas-sive crosslinkers and active molecular motors. Among these filament types, IFs are expressed in a cell-type specific manner and vimentin is found in cells of mesenchymal origin. The composite cytoskeletal network determines the mechanical and dynamic properties of the cell and is specifically governed by the interplay of the three different filament systems. We study the influence of vimentin IFs on the mechanics and net-work structure of microtubules by analyzing fluorescence micrographs of fibroblasts on protein micropatterns. We develop and apply quantitative, automated data analysis to a large number of cells, thus mitigating the considerable natural variance in data from biological cells. We find that the presence of a vimentin IF network structures and aligns microtubules in the cell interior. On a local scale, we observe higher micro-tubule curvatures when vimentin IFs are present, irrespective of whether the cells are polarized or not. Our results suggest that the vimentin IF network laterally supports microtubules against compressive buckling forces and further helps to structure the microtubule network, thus possibly leading to a more efficient intracellular transport system along the microtubules.

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Section: Discussionsupporting

confidence: 91%

Vimentin intermediate filaments structure and mechanically support microtubules in cells

Blob

Ventzke

Nies

et al. 2023

Preprint

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“…Motor accumulation results in an increased time of microtubule pausing at the cell periphery and this, in turn, results in microtubule bending, looping, and buckling (Figure 3). Microtubule bending and buckling occurs in response to compressive loads but does not normally lead to microtubule breakage and fragmentation [61][62][63][64][65][66][67][68]. We suggest that the excessive damage caused by the KIF5C(1-560)-D6 variant results in microtubules that break under compressive loads.…”

Section: Kinesin-1 Motor Activity Causes Microtubule Fragmentation In...mentioning

confidence: 84%

A kinesin-1 variant reveals motor-induced microtubule damage in cells

et al. 2022

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Section: Kinesin-1 Motor Activity Causes Microtubule Fragmentation In Cellsmentioning

confidence: 99%

A kinesin-1 variant reveals motor-induced microtubule damage in cells

Budaitis

Badieyan

Yue

et al. 2021

Preprint

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Kinesins drive the transport of cellular cargoes as they walk along microtubule tracks, however, recent work has suggested that the physical act of kinesins walking along microtubules can stress the microtubule lattice. Here, we describe a kinesin-1 KIF5C mutant with an increased ability to generate defects in the microtubule lattice as compared to the wild-type motor. Expression of the mutant motor in cultured cells resulted in microtubule breakage and fragmentation, suggesting that kinesin-1 variants with increased damage activity would have been selected against during evolution. The increased ability to damage microtubules is not due to the altered motility properties of the mutant motor as expression of the kinesin-3 motor KIF1A, which has similar single-motor motility properties, also caused increased microtubule pausing, bending, and buckling but not breakage. In cells, motor-induced microtubule breakage could not be prevented by increased α-tubulin K40 acetylation, a post-translational modification known to increase microtubule flexibility. In vitro, lattice damage induced by wild-type KIF5C was repaired by soluble tubulin and resulted in increased rescues and microtubule growth whereas lattice damage induced by the KIF5C mutant resulted in larger repair sites that made the microtubule vulnerable to breakage and fragmentation when under mechanical stress. These results demonstrate that kinesin-1 motility causes defects in and damage to the microtubule lattice in cells. While cells have the capacity to repair lattice damage, conditions that exceed this capacity result in microtubule breakage and fragmentation and may contribute to human disease.

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Characterization of microtubule buckling in living cells

Cited by 12 publications

References 42 publications

Vimentin intermediate filaments structure and mechanically support microtubules in cells

Vimentin intermediate filaments structure and mechanically support microtubules in cells

A kinesin-1 variant reveals motor-induced microtubule damage in cells

A kinesin-1 variant reveals motor-induced microtubule damage in cells

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