Bidirectional Interplay between Vimentin Intermediate Filaments and Contractile Actin Stress Fibers

Abstract

The actin cytoskeleton and cytoplasmic intermediate filaments contribute to cell migration and morphogenesis, but the interplay between these two central cytoskeletal elements has remained elusive. Here, we find that specific actin stress fiber structures, transverse arcs, interact with vimentin intermediate filaments and promote their retrograde flow. Consequently, myosin-II-containing arcs are important for perinuclear localization of the vimentin network in cells. The vimentin network reciprocally restricts retrograde movement of arcs and hence controls the width of flat lamellum at the leading edge of the cell. Depletion of plectin recapitulates the vimentin organization phenotype of arc-deficient cells without affecting the integrity of vimentin filaments or stress fibers, demonstrating that this cytoskeletal cross-linker is required for productive interactions between vimentin and arcs. Collectively, our results reveal that plectin-mediated interplay between contractile actomyosin arcs and vimentin intermediate filaments controls the localization and dynamics of these two cytoskeletal systems and is consequently important for cell morphogenesis.

An Atypical Tropomyosin in Drosophila with Intermediate Filament-like Properties

“…One hypothesis is that cytoplasmic Tm1-I/C is necessary to localize canonical Tms to the appropriate part of the cell where stress fibers form, as has been described for vimentin (Jiu et al, 2015). To test the effect of Tm1-I/C on the subcellular localization of Tm1-A, we expressed them in S2 cells.…”

“…For example, association of vimentin with focal adhesions stabilizes them (Burgstaller et al, 2010). Mutual dependence of vimentin and nestin IFs and F-actin stress fibers also occurs in osteosarcoma cells (Jiu et al, 2015). …”

Selective regulation of Notch ligands during angiogenesis is mediated by vimentin

“…The vimentin IF has been shown to act as a scaffold for signaling proteins that regulate epithelial mesenchymal transition (EMT), cancer cell invasion, wound healing and tissue repair, tissue aging, as well as inflammatory signaling (3,4,(6)(7)(8)10). Vimentin anchors and organizes adhesion molecules as well as actomyosin complexes (15) to regulate cell adhesion and migration (4,5). Vimentin also influences protein function through regulation of protein trafficking and is involved in the regulation of gene expression (7,8,10,(16)(17)(18).…”

The lens actin filament cytoskeleton: Diverse structures for complex functions

“…Ezrin-radixin-moesin (ERM) proteins, which link actin filament networks to the plasma membrane (Bretscher et al, 2000) and interact with N-WASP, an activator of Arp2/3-nucleated actin assembly (Manchanda et al, 2005), are present in the lens (Bagchi et al, 2004; Ingraffea et al, 2002; Rao et al, 2008; Straub et al, 2003). Immunoprecipitation experiments (Straub et al, 2003) indicate that plectin may serve as an important linker between ERM proteins, intermediate filament (Wiche et al, 2015; Wiche and Winter, 2011) and actin filament networks (Andra et al, 1998; Fontao et al, 2001; Jiu et al, 2015) in the lens. A recent study indicates that polymorphisms and genetic variations in ezrin are linked to human age-related cataracts (Lin et al, 2013), but the mechanism for these opacities and any links to the actin cytoskeleton will require further study.…”