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. 2014 Jun 3;5:131. doi: 10.3389/fphar.2014.00131

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Copyright © 2014 Agarwal.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Mechanisms of TGFβ activation by αvβ6 integrin. (A) LAP forms a straightjacket around TGFβ in the small latent complex (SLC) and binds to LTBP to for the large latent complex (LLC). The LTBP is in turn tethered to the extracellular matrix. (B) The cell associated αvβ6 integrin binds to the RGD domains of LAP, pulling the LAP ope against the resistance provided by the extracellular matrix/LTBP interaction. (C) TGFβ is then released from the LAP, allowing it to interact with its receptor.