... was associated with a heterogenous downregulation of vimentin (VIM) expression and a lack of coordination in collective behaviors, such as wound healing and acinus morphogenesis. Re-expression of vimentin in triple KO cells largely restored normal persistence of single cell migration, suggesting that vimentin...

... physical proximity to vimentin IFs in cultured mouse and human cells. We also show that the trans -Golgi network coiled-coil protein GORAB can physically associate with vimentin IFs. Loss of vimentin and/or GORAB had a modest effect upon Golgi structure at the steady state. The Golgi underwent more rapid...

..., host cytoskeletal networks constantly interact with bacteria and are integral to their uptake. Vimentin, an intermediate filament protein, is one such cytoskeletal component that interacts with bacteria during infection. Although vimentin is predominantly present in the cytoplasm, it also appears...

...Lei Qi; Teresa Knifley; Min Chen; Kathleen L. O'Connor ABSTRACT Integrin α6β4 binds plectin to associate with vimentin; however, the biological function remains unclear. Here, we utilized various integrin β4 mutants and CRISPR-Cas9 editing to investigate this association. Upon laminin binding...

...Zofia Ostrowska-Podhorodecka; Isabel Ding; Wilson Lee; Jelena Tanic; Sevil Abbasi; Pamma D. Arora; Richard S. Liu; Alison E. Patteson; Paul A. Janmey; Christopher A. McCulloch ABSTRACT Vimentin is a structural protein that is required for mesenchymal cell migration and directly interacts with actin...

...Yue Zhang; Zeyu Wen; Xuemeng Shi; Yan-Jun Liu; John E. Eriksson; Yaming Jiu ABSTRACT Epidemics caused by viral infections pose a significant global threat. Cytoskeletal vimentin is a major intermediate filament (IF) protein, and is involved in numerous functions, including cell signaling...

...Zachary T. Colburn; Jonathan C. R. Jones ABSTRACT We find that clusters of β4 integrin, organized into distinct puncta, localize along vimentin filaments within lamellipodia at the cell edge of A549 cells, as assessed by interferometric photoactivated localization microscopy. Moreover, puncta...

... associate with each other, but the underlying mechanisms of this interaction are incompletely understood. Here, we show that inactivation of vimentin leads to increased actin stress fiber assembly and contractility, and consequent elevation of myosin light chain phosphorylation and stabilization...

..., with the vimentin intermediate filament and microtubule cytoskeletons in naive cells . In vitro binding studies showed that MAP2D bound directly to vimentin and β-tubulin. Phosphorylation of recombinant MAP2D on Thr256 and Thr259, which mimics the phosphorylation status of MAP2D in naive cells, reduces binding...

...Jiyoon Kim; Chansik Yang; Eun Jin Kim; Jungim Jang; Se-Jong Kim; So Min Kang; Moon Gyo Kim; Hosung Jung; Dongeun Park; Chungho Kim ABSTRACT Vimentin, an intermediate filament protein induced during epithelial-to-mesenchymal transition, is known to regulate cell migration and invasion. However...

... 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...

... activation of SH2 domain-containing phosphatase-2 (SHP2; also known as PTPN11), a proto-oncogene. In lung and pancreatic cancer cell lines, reductions in E-cadherin expression, increases in vimentin expression and increases in cell scatter rates were larger when cells were treated with TGFβ and EGF versus...

.... The intermediate filament protein vimentin is an inducer of migration and a marker for epithelial–mesenchymal transition. Given that keratin intermediate filaments are regulated by SPC, with consequences for cell motility, we wanted to determine whether vimentin is also regulated by sphingolipid signalling...

... recruitment of citron and myosin II to the plasma membrane of mitotic lymphocytes as well as Rock2-mediated phosphorylation of vimentin, which is crucial to maintain the stiffness and shape of lymphocytes. In addition to its effects on cell shape, silencing of ARHGAP19 in lymphocytes also impairs chromosome...

.... In contrast, the passenger strand miR-17-3p repressed expression of vimentin, an intermediate filament with the ability to modulate metabolism, and GalNT7, an enzyme that regulates metabolism of liver toxin galactosamine. Hepatocellular carcinoma cells, HepG2, transfected with miR-17 formed larger tumors...

... of vimentin filaments. A higher content of polymerized vimentin filaments was correlated with a lower content of podosome rosettes. Taken together, our findings indicate that SHP2 serves as a negative regulator of podosome rosette formation through the dephosphorylation of Tks5 and the activation of ROCK...

... and functions as an adapter, linking InsP 3 Rs to vimentin intermediate filaments. Upon epithelial differentiation, KRAP and vimentin are both required for InsP 3 R accumulation at the periphery of MDCK cells. Finally, KRAP associates with vimentin in chicken B lymphocytes and with keratins in a breast cancer...

... of vimentin IFs which interact with melanosomes. IFs form an intricate, honeycomb-like network that form cages surrounding individual and small clusters of melanosomes, both when they are aggregated and dispersed. Purified melanosome preparations contain a substantial amount of vimentin, suggesting...

...Roland Bornheim; Martin Müller; Uschi Reuter; Harald Herrmann; Heinrich Büssow; Thomas M. Magin Vimentin is the main intermediate filament (IF) protein of mesenchymal cells and tissues. Unlike other IF –/– mice, vimentin –/– mice provided no evidence of an involvement of vimentin...

...). TorsinA, a member of the AAA+ ATPase superfamily, is located within the lumen of the nuclear envelope (NE) and endoplasmic reticulum (ER). We investigated an association between torsinA and nesprin-3, which spans the outer nuclear membrane (ONM) of the NE and links it to vimentin via plectin...