Vimentin filaments interact with the actin cortex in mitosis allowing normal cell division

Duarte, Sofia; Viedma-Poyatos, Álvaro; Navarro-Carrasco, Elena; Martínez, Alma E.; Pajares, Marı́a A.; Pérez‐Sala, Dolores

doi:10.1038/s41467-019-12029-4

Cited by 100 publications

(109 citation statements)

References 68 publications

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“…Vimentin plays key roles in essential cell functions such as division and migration, and contributes to cellular structural support and plasticity and organelle positioning. In addition, recent reports have unveiled its complex interplay with other cytoskeletal systems [1,2] and its involvement in redox sensing [3,4], regulation of gene expression [5] or protection of the nucleus and DNA from damage [6]. Moreover, biophysical techniques are providing high resolution information on the mechanics and dynamic performance of the vimentin network, with clear impact on the physical properties of cells [6,7].…”

Section: Introductionmentioning

confidence: 99%

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Mónico¹,

Zorrilla²,

Rivas³

2020

Preprint

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The intermediate filament protein vimentin constitutes a critical sensor for electrophilic and oxidative stress. We previously showed that vimentin interacts with zinc, which affects its assembly and redox sensing. Here we have used vimentin wt and C328S, an oxidation-resistant mutant showing improved NaCl-induced polymerization, to assess the impact of zinc on soluble and polymerized vimentin by light scattering and electron microscopy. Zinc acts as a switch, reversibly inducing the formation of vimentin oligomeric species. High zinc concentrations elicit optically-detectable vimentin structures with a characteristic morphology depending on the support. These effects also occur in vimentin C328S, but are not mimicked by magnesium. Treatment of vimentin with micromolar zinc induces fibril-like particles that do not assemble into filaments, but form aggregates upon subsequent addition of NaCl. In contrast, when added to NaCl-polymerized vimentin, zinc increases the diameter or induces lateral association of vimentin wt filaments. Remarkably, these effects are absent or attenuated in vimentin C328S filaments. Therefore, the zinc-vimentin interaction depends on the chemical environment and on the assembly state of the protein, leading to atypical polymerization of soluble vimentin, likely through electrostatic interactions, or to broadening and lateral association of preformed filaments through mechanisms requiring the cysteine residue. Thus, impact of zinc on vimentin assembly and redox regulation is envisaged.

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Section: Introductionmentioning

confidence: 99%

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Mónico¹,

Zorrilla²,

Rivas³

2020

Preprint

Self Cite

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show abstract

“…Vimentin plays key roles in essential cell functions such as division and migration and contributes to cellular structural support and plasticity and organelle positioning. In addition, recent reports have unveiled its complex interplay with other cytoskeletal systems [1,2] and its involvement in redox sensing [3,4], regulation of gene expression, [5] or protection of the nucleus and DNA from damage [6]. Moreover, biophysical techniques are providing high resolution information on the mechanics and dynamic performance of the vimentin network, with a clear impact on the physical properties of cells [6,7].…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, biophysical techniques are providing high resolution information on the mechanics and dynamic performance of the vimentin network, with a clear impact on the physical properties of cells [6,7]. In pathophysiology, vimentin is a key marker and agent of epithelial mesenchymal transition and tumor malignancy [2,[8][9][10] and is involved in bacterial and viral infections [11] and autoimmune diseases [12].…”

Section: Introductionmentioning

confidence: 99%

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Mónico

Zorrilla

Rivas

2020

IJMS

Self Cite

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The intermediate filament protein vimentin constitutes a critical sensor for electrophilic and oxidative stress. We previously showed that vimentin interacts with zinc, which affects its assembly and redox sensing. Here, we used vimentin wt and C328S, an oxidation-resistant mutant showing improved NaCl-induced polymerization, to assess the impact of zinc on soluble and polymerized vimentin by light scattering and electron microscopy. Zinc acts as a switch, reversibly inducing the formation of vimentin oligomeric species. High zinc concentrations elicit optically-detectable vimentin structures with a characteristic morphology depending on the support. These effects also occur in vimentin C328S, but are not mimicked by magnesium. Treatment of vimentin with micromolar ZnCl2 induces fibril-like particles that do not assemble into filaments, but form aggregates upon subsequent addition of NaCl. In contrast, when added to NaCl-polymerized vimentin, zinc increases the diameter or induces lateral association of vimentin wt filaments. Remarkably, these effects are absent or attenuated in vimentin C328S filaments. Therefore, the zinc-vimentin interaction depends on the chemical environment and on the assembly state of the protein, leading to atypical polymerization of soluble vimentin, likely through electrostatic interactions, or to broadening and lateral association of preformed filaments through mechanisms requiring the cysteine residue. Thus, the impact of zinc on vimentin assembly and redox regulation is envisaged.

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“…Its manifold tasks depend on the fine-tuned interplay between the three filamentous components, actin filaments, microtubules and intermediate filaments (IFs). [1][2][3][4][5][6] For example, all three types of cytoskeletal polymers participate in cell migration, adhesion and division. [3][4][5][6] In particular, the interplay of IFs and microtubules makes and important contribution to cytoskeletal crosstalk, although the interaction mechanisms largely remain unclear.…”

mentioning

confidence: 99%

“…[1][2][3][4][5][6] For example, all three types of cytoskeletal polymers participate in cell migration, adhesion and division. [3][4][5][6] In particular, the interplay of IFs and microtubules makes and important contribution to cytoskeletal crosstalk, although the interaction mechanisms largely remain unclear. 1,[7][8][9][10][11][12][13][14][15][16][17][18] For instance, vimentin, one of the most abundant members of the IF family, forms closely associated parallel arrays with microtubules.…”

mentioning

confidence: 99%

Vimentin Intermediate Filaments Stabilize Dynamic Microtubules by Direct Interactions

Schaedel

Lorenz

Schepers

et al. 2020

Preprint

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The cytoskeleton determines cell mechanics and lies at the heart of important cellular functions. Growing evidence suggests that the manifold tasks of the cytoskeleton rely on the interactions between its filamentous components, known as actin filaments, intermediate filaments and microtubules. However, the nature of these interactions and their impact on cytoskeletal dynamics are largely unknown. Here, we show in a reconstituted in vitro system that vimentin intermediate filaments stabilize microtubules against depolymerization and support microtubule rescue. To understand these stabilizing effects, we directly measure the interaction forces between individual microtubules and vimentin filaments. Combined with numerical simulations, our observations provide detailed insight into the physical nature of the interactions and how they affect

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Vimentin filaments interact with the actin cortex in mitosis allowing normal cell division

Cited by 100 publications

References 68 publications

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Zinc Differentially Modulates the Assembly of Soluble and Polymerized Vimentin

Vimentin Intermediate Filaments Stabilize Dynamic Microtubules by Direct Interactions

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