Abstract
A variety of growth factors and hormones mediate their cellular affects via interactions with cell surface receptors that possess protein kinase activity (Williams, 1989; Ullrich and Schlessinger, 1990). The interaction of most of these ligands with their receptors induces tyrosine kinase activation and autophosphorylation of the receptor, resulting in physical association of the receptors with several cytoplasmic substrates having SH2 domains (Otsu et al., 1991; Skolnik et al., 1991). Phosphoinositide 3-kinase (PI3K) has been identified through its ability to associate with cellular protein kinases, including numerous growth factor receptors and oncogene products (Otsu et al., 1991; Skolnik et al., 1991).
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Rajala, R.V.S., McClellan, M.E., Ash, J.D., Anderson, R.E. (2003). Regulation of Retinal Phosphoinositide 3-Kinase Activity in p85α-Subunit Knockout Mice. In: LaVail, M.M., Hollyfield, J.G., Anderson, R.E. (eds) Retinal Degenerations. Advances in Experimental Medicine and Biology, vol 533. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0067-4_47
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DOI: https://doi.org/10.1007/978-1-4615-0067-4_47
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