Integrins are cell adhesion molecules that can mediate bidirectional transfer of signals across the plasma membrane. The cytoplasmic domains of integrin family members interact with components of the signal transduction apparatus within cells. Integrin α6β4receptors are found in basement membrane along with laminin-5. These receptors are expressed in epithelial, schwann, endothelial and some immune cells. The cytoplasmic domain of the Integrin β4 subunit recruits the adaptor protein Shc and is required for assembly of hemidesmosomes. Tyrosine phosphorylation of multiple sites within the cytoplasmic domain regulates these cellular events. In particular, tyrosine 1526 interacts with the phosphotyrosine binding domain of Shc and is required for Shc activation. In addition, tyrosine 1494 is required for integrin-mediated IRS-2 phosphorylation and activation of PI3-kinase. More importantly this site is critical for integrin α6β4 increases in carcinoma invasion.
Wang, L. et al. (2012) J Cell Physiol. 227(2):474.
Dans, M. et al. (2001). J Biol Chem. 276(2):1494-1502.
Shaw, L.M. (2001). Mol Cell Biol. 21(15):5082-5093.
*For more information, see UniProt Accession P16144
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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