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Review
. 2013 Jan 7;200(1):9-19.
doi: 10.1083/jcb.201210090.

The tension mounts: stress fibers as force-generating mechanotransducers

Keith Burridge  1 , Erika S Wittchen
Affiliations
Review

The tension mounts: stress fibers as force-generating mechanotransducers

Keith Burridge et al. J Cell Biol. .

Abstract

Stress fibers (SFs) are often the most prominent cytoskeletal structures in cells growing in tissue culture. Composed of actin filaments, myosin II, and many other proteins, SFs are force-generating and tension-bearing structures that respond to the surrounding physical environment. New work is shedding light on the mechanosensitive properties of SFs, including that these structures can respond to mechanical tension by rapid reinforcement and that there are mechanisms to repair strain-induced damage. Although SFs are superficially similar in organization to the sarcomeres of striated muscle, there are intriguing differences in their organization and behavior, indicating that much still needs to be learned about these structures.

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Figures

Figure 1.
Figure 1.
Three types of actin SFs. U2OS human osteosarcoma cells were plated on 10 µg/ml fibronectin-coated coverslips and allowed to attach and spread for 4 h before fixation (Hotulainen and Lappalainen, 2006). In the immunofluorescence image, antiphosphotyrosine was used as a marker for focal adhesions (red), phalloidin was used for F-actin SFs (green), and the nucleus (blue) was detected by DAPI. This single cell exhibits the three main types of actin SFs: (transverse) arcs, dorsal SFs, and ventral SFs. (inset) Schematic drawing depicting the SF subtypes.
Figure 2.
Figure 2.
Endothelial cell junctional F-actin structures. Human umbilical vein endothelial cells grown as confluent monolayers were fixed and stained for β-catenin to identify cell junctions and phalloidin to label F-actin. (A) Example of cortical actin belts. This cell demonstrates a strong cortical enrichment of F-actin, arranged parallel to cell junctions. Bars, 15 µm. (B) Example of inserted junctional SFs. Another cell exhibits several discontinuous junctions (indicated by asterisks in enlarged merged image), where the insertion of SF ends can be observed. These junctions appear to physically connect SFs between two adjacent endothelial cells. Boxed areas show the area enlarged below. Bars, 25 µm.
Figure 3.
Figure 3.
Periodicity of α-actinin within SFs. Swiss 3T3 cells stably expressing GFP–α-actinin (Edlund et al., 2001) were fixed and labeled with Texas red–phalloidin to label F-actin. Note the variable dimensions and spacing of the periodic fluorescence of GFP-tagged α-actinin along the length of SFs (red). Bar, 25 µm. (inset) Enlarged view of the boxed area. Bar, 10 µm.
Figure 4.
Figure 4.
Proposed model for conversion of unipolar to bidirectional actin filaments during the maturation of SFs. Unipolar, α-actinin cross-linked actin filament bundles oriented with their barbed ends facing the focal adhesion are first severed and capped (step 1). This severing protein then either recruits another protein or protein complex that nucleates actin filament polymerization in the opposite orientation, or alternatively, a single protein possessing severing/capping/nucleation activity may fulfill this role (step 2). The final stage involves incorporation of myosin filaments into the maturing SF with its characteristic periodic distribution (step 3).
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References

    1. Abercrombie M., Heaysman J.E., Pegrum S.M. 1971. The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp. Cell Res. 67:359–367 10.1016/0014-4827(71)90420-4 - DOI - PubMed
    1. Adamson P., Etienne S., Couraud P.O., Calder V., Greenwood J. 1999. Lymphocyte migration through brain endothelial cell monolayers involves signaling through endothelial ICAM-1 via a rho-dependent pathway. J. Immunol. 162:2964–2973 - PubMed
    1. Amano M., Ito M., Kimura K., Fukata Y., Chihara K., Nakano T., Matsuura Y., Kaibuchi K. 1996. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271:20246–20249 10.1074/jbc.271.34.20246 - DOI - PubMed
    1. Arthur W.T., Petch L.A., Burridge K. 2000. Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10:719–722 10.1016/S0960-9822(00)00537-6 - DOI - PubMed
    1. Bakin A.V., Safina A., Rinehart C., Daroqui C., Darbary H., Helfman D.M. 2004. A critical role of tropomyosins in TGF-beta regulation of the actin cytoskeleton and cell motility in epithelial cells. Mol. Biol. Cell. 15:4682–4694 10.1091/mbc.E04-04-0353 - DOI - PMC - PubMed

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