Regulation of Retinal Phosphoinositide 3-Kinase Activity in p85α-Subunit Knockout Mice
作者： Raju V. S. Rajala , Mark E. McClellan , John D. Ash , Robert E. Anderson
DOI: 10.1007/978-1-4615-0067-4_47
关键词: Protein kinase A 、 Receptor 、 Tyrosine kinase 、 Cell surface receptor 、 SH2 domain 、 Kinase 、 Growth factor receptor 、 Cell biology 、 Autophosphorylation 、 Chemistry
摘要: 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 Schlessinger, 1990). The interaction most these ligands induces tyrosine activation autophosphorylation the receptor, resulting in physical association several cytoplasmic substrates having SH2 domains (Otsu et al., 1991; Skolnik 1991). Phosphoinositide 3-kinase (PI3K) has been identified through its ability to associate kinases, including numerous factor oncogene products
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