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. Author manuscript; available in PMC: 2014 Jul 1.
Published in final edited form as: Biochim Biophys Acta. 2013 Feb 20;1832(7):884–890. doi: 10.1016/j.bbadis.2013.02.007

Figure 2.

Figure 2

The role of mechanics in TGF-β activation. TGF-β is released in latent form, enclosed within the latency-associated peptide (LAP) as part of the TGF-β latent complex. Cell surface integrins, which connect to cytoplasmic actins at the site of focal adhesions, bind to LAP. As shown by Hinz and colleagues [36, 37], on soft surfaces (left) there is minimal resistance to cell generated tension and the complex remains latent. On stiff surfaces (right), there is significant resistance to cell-generated tension, this tension increases, and the LAP is pulled open, releasing active TGF-β.