AI Article Synopsis
- The review examines the structural and functional roles of the p55/p85 regulatory and p110 catalytic subunits of phosphatidylinositol-3-kinases (PI-3-kinases).
- The author discusses how these subunits interact with insulin and growth factor signaling components, including models of their interaction with insulin receptor substrate proteins.
- Emphasis is placed on the mechanisms behind the functional connections between the regulatory and catalytic subunits, particularly highlighting the potential role of coiled-coil interactions.
Article Abstract
This review presents literary data and results of the author own studies on structural and functional characteristics of regulatory (p55/p85) and catalytic (p110) subunits of heterodimeric phosphatidylinositol-3-kinases (PI-3-kinases), and on molecular mechanisms of their functional conjugation with other signaling system components, regulated by insulin and growth factors. Various models simulating the interaction of regulatory subunits of PI-3-kinase and of their substrates (insulin receptor sustrate proteins phosphorylated on tyrosin residues) with molecules of receptors-tyrosinekinases have been considered. Mechanisms of the functional conjugation between regulatory and catalytic enzyme subunits are discussed, with special reference to a possible role of the coiled-coil interactions in this process.
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