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• W2215679030 abstract "Mutations in the cytoskeletal linker protein plectin result in multisystemic diseases affecting skin and muscle with indications of additional vascular system involvement. To study the mechanisms underlying vascular disorders, we established plectin-deficient endothelial cell and mouse models. We show that apart from perturbing the vimentin cytoskeleton of endothelial cells, plectin deficiency leads to severe distortions of adherens junctions (AJs) as well as tight junctions, accompanied by an upregulation of actin stress fibres and increased cellular contractility. Plectin-deficient endothelial cell layers were leakier and showed reduced mechanical resilience in fluid-shear stress and mechanical stretch experiments. We imply that distorted AJs and upregulated actin stress fibres in plectin-deficient cells are rooted in perturbations of the vimentin cytoskeleton as similar phenotypes could be mimicked in wild-type cells by disruption of vimentin filaments. In vivo studies in endothelium-restricted conditional plectin knockout mice revealed significant distortions of AJs in stress prone aortic arch regions and increased pulmonary vascular leakage. Our study opens a new perspective on cytoskeleton-controlled vascular permeability, where a plectin-organized vimentin scaffold keeps actomyosin contractility “in-check” and maintains AJ homeostasis." @default.
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• W2215679030 date "2015-01-01" @default.
• W2215679030 modified "2023-10-05" @default.
• W2215679030 title "Plectin reinforces vascular integrity by mediating vimentin-actin network crosstalk" @default.
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• W2215679030 doi "https://doi.org/10.1242/jcs.172056" @default.
• W2215679030 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4712781" @default.
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