Vimentin supports cell polarization by enhancing centrosome function and microtubule acetylation

Saldanha, Renita; Thanh, Minh Tri Ho; Krishnan, Nikhila; Hehnly, Heidi; Patteson, Alison E.

doi:10.1101/2023.02.17.528977

Cited by 4 publications

(4 citation statements)

References 48 publications

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“…In fact, pericentrin depletion has been shown to disrupt cilia formation in human retinal epithelial (RPE1) cells [41]. Our observations are consistent with a recent report indicating that vimentin “mediates” the structure of the pericentriolar material and its absence correlates with a decrease of pericentrin at the centrosome [50]. On the other hand, elevated pericentrin, as observed in trisomy 21 delays primary ciliogenesis by disrupting multiple early steps of this process, and decreases sonic hedgehog signaling [40].…”

Section: Discussionsupporting

confidence: 91%

“…Vimentin overexpression has been reported to decrease α-tubulin acetylation levels in HeLa cells [49]. On the other hand, vimentin appears to increase and stabilize acetylated microtubules in MEF [50]. In migrating astrocytes, vimentin filaments have been reported to dampen a positive feedback loop between microtubule acetylation and Rho-driven actomyosin contractility, [51].…”

Section: Discussionmentioning

confidence: 99%

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Key role of vimentin in the organization of the primary cilium

Lalioti,

Moneo-Corcuera,

Pérez-Sala

2024

Preprint

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We previously reported the presence of the intermediate filament vimentin at the primary cilium of lung cancer epithelial cells. In this study we further demonstrate that vimentin is intimately intertwined with acetylated tubulin at this structure. Interestingly, although vimentin can be detected along the whole length of the primary cilium, phospho-serine 56 vimentin is found particularly enriched at its basal region in A549 lung cancer cells. Vimentin appears to play a pivotal role in ciliogenesis, since its depletion in MEF or in A549 cells results in a lower proportion of cells displaying primary cilia and recognizable basal bodies. Furthermore, the detectable cilia in vimentin depleted cells are shorter. In addition, the centriolar structure appears disrupted in vimentin deficient cells, as indicated by an abnormal distribution of gamma- and acetylated tubulin. Moreover, these cells display a defective organization of the pericentriolar material, characterized by a marked decrease in the levels of pericentrin and a diffuse distribution of Rab11. Taken together, our results show that vimentin is present at the primary cilium and suggest that it plays an important role in cilium structure and biogenesis, since its depletion leads to marked morphological defects and altered organization of key elements of this structure.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Key role of vimentin in the organization of the primary cilium

Lalioti,

Moneo-Corcuera,

Pérez-Sala

2024

Preprint

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“…Data accessibility. All data can be accessed from the Dryad digital repository [64]. Electronic supplementary material is available online [65].…”

Section: Discussionmentioning

confidence: 99%

Vimentin supports cell polarization by enhancing centrosome function and microtubule acetylation

Saldanha,

Ho Thanh,

Krishnan

et al. 2024

J. R. Soc. Interface.

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Cell polarity is important for controlling cell shape, motility and cell division processes. Vimentin intermediate filaments are important for cell migration and cell polarization in mesenchymal cells and assembly of vimentin and microtubule networks is dynamically coordinated, but the precise details of how vimentin mediates cell polarity remain unclear. Here, we characterize the effects of vimentin on the structure and function of the centrosome and the stability of microtubule filaments in wild-type and vimentin-null mouse embryonic fibroblasts. We find that vimentin mediates the structure of the pericentriolar material, promotes centrosome-mediated microtubule regrowth and increases the level of stable acetylated microtubules in the cell. Loss of vimentin also impairs centrosome repositioning during cell polarization and migration processes that occur during wound closure. Our results suggest that vimentin modulates centrosome structure and function as well as microtubule network stability, which has important implications for how cells establish proper cell polarization and persistent migration.

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“…6B. Vimentin is known to increase cell polarization through its interactions with microtubules and actomyosin networks [64–69]. Interestingly, we have found when cells are geometrically constrained to polarized shapes on micropatterned substrates, vimentin increases the transmission of internal acto-myosin based forces to the cell nucleus, leading to larger deformations and elongations of the nucleus [70].…”

Section: Discussionmentioning

confidence: 99%

Vimentin promotes collective cell migration through collagen networks via increased matrix remodeling and spheroid fluidity

Thanh,

Poudel,

Ameen

et al. 2024

Preprint

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The intermediate filament (IF) protein vimentin is associated with many diseases with phenotypes of enhanced cellular migration and aggressive invasion through the extracellular matrix (ECM) of tissues, but vimentin’s role in in-vivo cell migration is still largely unclear. Vimentin is important for proper cellular adhesion and force generation, which are critical to cell migration; yet the vimentin cytoskeleton also hinders the ability of cells to squeeze through small pores in ECM, resisting migration. To identify the role of vimentin in collective cell migration, we generate spheroids of wide-type and vimentin-null mouse embryonic fibroblasts (mEFs) and embed them in a 3D collagen matrix. We find that loss of vimentin significantly impairs the ability of the spheroid to collectively expand through collagen networks and remodel the collagen network. Traction force analysis reveals that vimentin null spheroids exert less contractile force than their wild-type counterparts. In addition, spheroids made of mEFs with only vimentin unit length filaments (ULFs) exhibit similar behavior as vimentin-null spheroids, suggesting filamentous vimentin is required to promote 3D collective cell migration. We find the vimentin-mediated collective cell expansion is dependent on matrix metalloproteinase (MMP) degradation of the collagen matrix. Further, 3D vertex model simulation of spheroid and embedded ECM indicates that wild-type spheroids behave more fluid-like, enabling more active pulling and reconstructing the surrounding collagen network. Altogether, these results signify that VIF plays a critical role in enhancing migratory persistence in 3D matrix environments through MMP transportation and tissue fluidity.

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Vimentin supports cell polarization by enhancing centrosome function and microtubule acetylation

Cited by 4 publications

References 48 publications

Key role of vimentin in the organization of the primary cilium

Key role of vimentin in the organization of the primary cilium

Vimentin supports cell polarization by enhancing centrosome function and microtubule acetylation

Vimentin promotes collective cell migration through collagen networks via increased matrix remodeling and spheroid fluidity

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