Regulation of the Association of α6β4 with Vimentin Intermediate Filaments in Endothelial Cells

Homan, Suzanne M.

doi:10.1016/s0014-4827(02)95643-0

Cited by 14 publications

(20 citation statements)

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“…Plectin in endothelial cells plays an important role in linking vimentin intermediate filaments to α6β4 integrin by binding to the cytoplasmic tail of the β4 subunit (Homan et al 2002). We found that thiolutin significantly decreases plectin-1 association with Hsp27.…”

Section: Discussionmentioning

confidence: 70%

Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton

Jia

Isenberg

et al. 2010

Cell Stress and Chaperones

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Section: Discussionmentioning

confidence: 70%

Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton

Jia

Isenberg

et al. 2010

Cell Stress and Chaperones

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“…Because CHO cells are epithelial in origin, we examined the role of integrin-regulated ERK-RSK signaling in cytokinesis in the human mammary epithelial cell line MCF-10A. For these experiments, mitotic MCF10A cells were isolated from logarithmically growing cultures and either replated on a laminin-rich matrix (Homan et al, 2002;Langhofer et al, 1993) or incubated in suspension and the progression through cytokinesis was analyzed at 2.5 and 5 hours. Cells adhered to laminin-rich matrices exhibited robust activation of ERK and RSK; however, ERK and RSK activity were dramatically downregulated in suspended MCF10A cells at both 2.5 and 5 hours (Fig.…”

Section: Activated Rsk Partially Rescues Cytokinesis In Ya Cellsmentioning

confidence: 99%

“…Cells were fixed and stained and then analyzed for progression through cytokinesis by immunofluorescence microscopy. To compare cytokinesis success in adhered and suspended cells, mitotic MCF10A cells were isolated and either plated on a laminin-5-rich matrix (Homan et al, 2002) for 2.5 and 5 hours or left in suspension with intermittent shaking for 2.5 and 5 hours. The suspended cells were then plated on poly-lysine for 5 minutes and then analyzed as above.…”

Section: Cytokinesis Assaymentioning

confidence: 99%

Integrins Promote Cytokinesis through the RSK Signaling Axis

Mathew

Nieves

Sequeira

et al. 2013

Journal of Cell Science

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Cytokinesis is the final stage in cell division. Although integrins can regulate cytokinesis, the mechanisms involved are not fully understood. In this study, we demonstrate that integrin-regulated ERK (extracellular signal-related kinase) and RSK (p90 ribosomal S6 kinase) signaling promotes successful cytokinesis. Inhibiting the activation of ERK and RSK in CHO cells by a mutation in the integrin b1 cytoplasmic tail or with pharmacological inhibitors results in the accumulation of cells with midbodies and the formation of binucleated cells. Activation of ERK and RSK signaling by the expression of constitutively active RAF1 suppresses the mutant phenotype in a RSK-dependent manner. Constitutively active RSK2 also restores cytokinesis inhibited by the mutant integrin. Importantly, the regulatory role of the RSK pathway is not specific to CHO cells. MCF-10A human mammary epithelial cells and HPNE human pancreatic ductal epithelial cells exhibit a similar dependence on RSK for successful cytokinesis. In addition, depriving mitotic MCF10A cells of integrin-mediated adhesion by incubating them in suspension suppressed ERK and RSK activation and resulted in a failure of cytokinesis. Furthermore, inhibition of RSK or integrins within the 3D context of a developing salivary gland organ explant also leads to an accumulation of epithelial cells with midbodies, suggesting a similar defect in cytokinesis. Interestingly, neither ERK nor RSK regulates cytokinesis in human fibroblasts, suggesting cell-type specificity. Taken together, our results identify the integrin-RSK signaling axis as an important regulator of cytokinesis in epithelial cells. We propose that the proper interaction of cells with their microenvironment through integrins contributes to the maintenance of genomic stability by promoting the successful completion of cytokinesis.

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“…5A) may elicit Rab11-dependent pathways, thereby enhancing the efficacy of integrin recycling. In addition, alpha6beta4 integrin associates with vimentin intermediate filaments through the cytoplasmic tail of ITGB4 in a ligand-independent fashion (72). Phosphorylation of vimentin by protein kinase C within the recycling integrin compartment is crucial for the integrin trafficking through the cell (73), and this phosphorylation also regulates vimentin interaction with Rab9 and hence affects intracellular lipid transport (74,75).…”

Section: Elevated Levels Of Pra1-affected Proteins In Lmp1-expressingmentioning

confidence: 99%

Proteome-wide Dysregulation by PRA1 Depletion Delineates a Role of PRA1 in Lipid Transport and Cell Migration

Liu

Kao

et al. 2011

Molecular & Cellular Proteomics

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We have previously identified prenylated Rab acceptor 1 (PRA1) as a novel cellular interacting partner for EpsteinBarr virus-encoded oncoprotein, latent membrane protein 1 (LMP1). The intracellular trafficking and full signaling of LMP1 requires its interaction with PRA1. To further explore the role of PRA1 in Epstein-Barr virus-associated nasopharyngeal carcinoma (NPC) cells, we generated several PRA1-knockdown cell clones, which exhibited altered cell morphology and increased cell motility. We identified proteins differentially expressed in the knockdown clones by means of isobaric mass tags labeling coupled with multidimensional liquid chromatographymass spectrometry. We validated a panel of proteins, which showed consistent up-regulation in PRA1-knockdown clones and participated in regulating lipid homeostasis and cell migration. Immunofluorescence staining further revealed altered localization of these proteins and accumulation of intracellular cholesterol in PRA1-knockdown clones. These effects were phenocopied by treatment with a cholesterol transport inhibitor, U18666A. Moreover, overexpressed PRA1 was able to alleviate the dysregulation of these affected proteins either from PRA1 knockdown or U18666A treatment, implying a role for PRA1 in regulating the levels of these affected proteins in response to altered cholesterol homeostasis. We further demonstrated that LMP1 expression caused PRA1 sequestration in NPC cells, leading to a consequence reminiscent of PRA1 knockdown. Finally, the immunohistochemistry showed a physiological relevance of the PRA1-associated proteome-wide changes in NPC biopsy tissues. In sum, our findings delineated novel roles of PRA1 in lipid transport and cell migration, and provided additional insights into the molecular basis of NPC morphogenesis, namely a consequence of LMP1-PRA1 interaction.

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Regulation of the Association of α6β4 with Vimentin Intermediate Filaments in Endothelial Cells

Cited by 14 publications

References 0 publications

Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton

Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton

Integrins Promote Cytokinesis through the RSK Signaling Axis

Proteome-wide Dysregulation by PRA1 Depletion Delineates a Role of PRA1 in Lipid Transport and Cell Migration

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