Vimentin organization modulates the formation of lamellipodia

Helfand, Brian T.; Mendez, Melissa G.; Murthy, S. N. Prasanna; Shumaker, Dale K.; Grin, Boris; Mahammad, Saleemulla; Aebi, Ueli; Wedig, Tatjana; Wu, Yi; Hahn, Klaus M.; Inagaki, Masaki; Herrmann, Harald; Goldman, Robert D.

doi:10.1091/mbc.e10-08-0699

Cited by 243 publications

(316 citation statements)

References 73 publications

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“…Although diverse roles for vimentin in migration have been proposed (Havel et al, 2014;Helfand et al, 2011;Liu et al, 2015;Lowery et al, 2015;Mendez et al, 2010;Menko et al, 2014;Nieminen et al, 2006;Schoumacher et al, 2010), a systematic and quantitative analysis of VIF organization and dynamics in the context of cell migration has been lacking. Here, we establish, by high-resolution, multi-spectral live-cell imaging of genome edited cells expressing endogenous levels of fluorescent vimentin and α-tubulin, that VIF promotes directed cell migration as a polarity maintenance factor.…”

Section: Discussionmentioning

confidence: 99%

“…Because of the dependence of VIF assembly on the microtubule structure, such cues also lead to a reorganization of the VIF structure. Moreover, it is possible that cues which reorganize microtubules, may transiently destabilize VIF to lower the structural constraints imposed by VIF's templating function (Helfand et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…For vimentin the N-terminal addition of EGFP or mEmerald had previously been shown to yield functional fusion proteins (Helfand et al, 2011;Yoon et al, 1998); and α-tubulin was successfully labeled by Nterminal fusion of various fluorescent proteins in a variety of mammalian cells (reviewed here (Goodson et al, 2010)). To stably express the fusion proteins and to avoid artefacts from over-expression we chose to use a TALEN based genome editing approach to label the endogenous proteins.…”

Section: Genome Editing Of Memerald-vimentin and Mtagrfpt-tubulinmentioning

confidence: 99%

“…Nocodazole was dissolved in DMSO as 830 μM stock and kept at −20 °C until use. For mEmerald-Vimentin overexpression experiment, parental hTERT-RPE-1 cells were transiently transfected with the mEmerald-vimentin plasmid (Helfand et al, 2011) using Lipofectamin 2000 (Life Technologies). Transfection was done according to the manufacturer's manual.…”

Section: Live Cell Imagingmentioning

confidence: 99%

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Vimentin Intermediate Filaments Template Microtubule Networks to Enhance Persistence in Cell Polarity and Directed Migration

Gan¹,

Ding²,

Burckhardt³

et al. 2016

Cell Systems

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SUMMARYIncreased expression of vimentin intermediate filaments (VIF) enhances directed cell migration, but the mechanism behind VIF's effect on motility is not understood. VIF interact with microtubules, whose organization contributes to polarity maintenance in migrating cells. Here we characterize the dynamic coordination of VIF and microtubule networks in wounded monolayers of Retinal Pigment Epithelial cells. By genome editing we fluorescently labelled endogenous vimentin and α-tubulin and we developed computational image analysis to delineate architecture and interactions of the two networks. Our results show that VIF assemble an ultrastructural copy of the previously polarized microtubule network. Because the VIF network is long-lived compared to the microtubule network, VIF template future microtubule growth along previous microtubule tracks, thus providing a feedback mechanism that maintains cell polarity. VIF knockdown prevents cells from polarizing and migrating properly during wound healing. We suggest that VIF's templating function establishes a memory in microtubule organization that enhances persistence in cell polarization in general and migration in particular.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Genome Editing Of Memerald-vimentin and Mtagrfpt-tubulinmentioning

confidence: 99%

Section: Live Cell Imagingmentioning

confidence: 99%

See 2 more Smart Citations

Vimentin Intermediate Filaments Template Microtubule Networks to Enhance Persistence in Cell Polarity and Directed Migration

Gan¹,

Ding²,

Burckhardt³

et al. 2016

Cell Systems

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“…It is well known that brain development involves multiple processes and dynamic changes, for which various proteins are required. Several proteins are known to be involved in brain development, such as Fibronectin, Tenascin, Vimentin, Ncam [13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Differential Expression of Vimentin and GFAP Protein during Brain Development of Mouse Fetuses after Treated with 2-Methoxyethanol

Irnidayanti¹,

Darmanto²,

Abadi³

et al. 2012

itbj.sci.

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Abstract. 2-methoxyethanol or embryotoxic in animals cells and tissues in the body was performed using primary protein expressed was measured by techniques. The results show levels was higher (22.24% levels (15.10% on gestation day translation of Vimentin and cellular response to toxic materials. is essential for the development proliferation for cell repair Keywords: brain; cell repair cell response; 2-Methoxyethanol IntroductionThe objective of this research and GFAP expression during treatment with 7.5 mmol/kg intra-peritoneally on gestation methoxyethanol (2-ME) glycol ether compounds derived compound is widely used

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Role of Intermediate Filaments in Cell Locomotion

Fujiwara

Mizuno

2017

Encyclopedia of Life Sciences

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Cell locomotion is essential for diverse pathophysiological processes, including embryogenesis, immune responses, wound healing and cancer metastasis. Intermediate filaments (IFs) are resilient cytoskeleton components that provide structural support and mechanical protection. Accumulating evidence suggests that IFs are dynamic structures that function as a scaffold for signalling networks, which regulate cell locomotion, shape change and mechanical responses. The dynamics of IFs are regulated by posttranslational modifications, crosstalk with other cytoskeletons and association with cell adhesion complexes. IFs differentially regulate cell locomotion, depending on the particular IF protein, the cell type, the cellular context and the mode of cell migration. In general, vimentin filaments promote and keratin filaments inhibit cell locomotion. These cytoplasmic IFs regulate cell locomotion by modulating the localisation and activity of signalling molecules and influencing the stability of cell–cell and cell–substrate adhesion complexes. Nuclear lamin‐A represses cell locomotion by stiffening the nucleus. Key Concepts Intermediate filaments (IFs) constitute the resilient cytoskeleton that provides structural support and protects cells from external forces. IFs function as a dynamic scaffold for signalling networks that regulate locomotion, shape change and mechanical responses. Cytoplasmic IFs are linked to desmosomes and hemidesmosomes at cell adhesion sites and linker of nucleoskeleton and cytoskeleton (LINC) complexes on the nuclear membrane. The reorganisation and dynamics of IFs are regulated by posttranslational modifications, crosstalk with other cytoskeletons and association with cell adhesion complexes. IFs differentially regulate cell locomotion, depending on the particular IF protein, the cell type, the cellular context and the mode of cell migration. Vimentin IFs generally promote cell locomotion by destabilising desmosomes, promoting focal adhesion maturation and affecting the activity of signalling molecules. Keratin IFs generally repress cell locomotion by stabilising desmosomes and hemidesmosomes and affecting the localisation and activity of signalling molecules. Nuclear lamin‐A represses cell locomotion by stiffening the nucleus. Keratin IFs and Rho signalling are mutually regulated, providing a feedback mechanism during mechanical responses.

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Vimentin organization modulates the formation of lamellipodia

Abstract: The disassembly and withdrawal of vimentin intermediate filaments (VIF) from the plasma membrane induces membrane ruffling and the formation of a lamellipodium. Conversely, lamellipodium formation is inhibited when VIF are present.

Cited by 243 publications

References 73 publications

Vimentin Intermediate Filaments Template Microtubule Networks to Enhance Persistence in Cell Polarity and Directed Migration

Vimentin Intermediate Filaments Template Microtubule Networks to Enhance Persistence in Cell Polarity and Directed Migration

Differential Expression of Vimentin and GFAP Protein during Brain Development of Mouse Fetuses after Treated with 2-Methoxyethanol

Role of Intermediate Filaments in Cell Locomotion

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