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10.1242/jcs.196881 http://scihub22266oqcxt.onion/10.1242/jcs.196881 C5358333!5358333!28096473     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28096473&cmd=llinks): Failed to open stream: HTTP request failed! 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Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA |pdf=|usr=}}{{28096473}} gab.com Text Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28096473 #FOAvip The actin and intermediate filament cytoskeletons contribute to numerous cellular processes, including morphogenesis, cytokinesis and migration. These two cytoskeletal systems 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 of tropomyosin-4.2 (see Geeves et al., 2015). The vimentin-knockout phenotypes can be rescued by re-expression of wild-type vimentin, but not by the non-filamentous ?unit length form? vimentin, demonstrating that intact vimentin intermediate filaments are required to facilitate the effects on the actin cytoskeleton. Finally, we provide evidence that the effects of vimentin on stress fibers are mediated by activation of RhoA through its guanine nucleotide exchange factor GEF-H1 (also known as ARHGEF2). Vimentin depletion induces phosphorylation of the microtubule-associated GEF-H1 on Ser886, and thereby promotes RhoA activity and actin stress fiber assembly. Taken together, these data reveal a new mechanism by which intermediate filaments regulate contractile actomyosin bundles, and may explain why elevated vimentin expression levels correlate with increased migration and invasion of cancer cells. Twit Text FOAVip Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28096473 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28096473 #FOAvip English Wikipedia <ref>{{Cite pmid|28096473}}</ref> Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA #MMPMID28096473 Jiu Y; Peränen J; Schaible N; Cheng F; Eriksson JE; Krishnan R; Lappalainen P J Cell Sci 2017[Mar]; 130 (5): 892-902 PMID28096473show ga The actin and intermediate filament cytoskeletons contribute to numerous cellular processes, including morphogenesis, cytokinesis and migration. These two cytoskeletal systems 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 of tropomyosin-4.2 (see Geeves et al., 2015). The vimentin-knockout phenotypes can be rescued by re-expression of wild-type vimentin, but not by the non-filamentous ?unit length form? vimentin, demonstrating that intact vimentin intermediate filaments are required to facilitate the effects on the actin cytoskeleton. Finally, we provide evidence that the effects of vimentin on stress fibers are mediated by activation of RhoA through its guanine nucleotide exchange factor GEF-H1 (also known as ARHGEF2). Vimentin depletion induces phosphorylation of the microtubule-associated GEF-H1 on Ser886, and thereby promotes RhoA activity and actin stress fiber assembly. Taken together, these data reveal a new mechanism by which intermediate filaments regulate contractile actomyosin bundles, and may explain why elevated vimentin expression levels correlate with increased migration and invasion of cancer cells. äVimentin intermediate filaments control actin stress fiber assembly th(epmc).pdf DeepDyve Pubget Overpricing