[Structure-functional characteristics of heterodimeric phosphatidylinositol-3-kinase and molecular mechanisms of its conjugation with other components of the signaling system].
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.
Shpakov
A O
AO
Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg. shpakov@hormone.ief.spb.su
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D019869:Phosphatidylinositol 3-Kinases / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D019869:Phosphatidylinositol 3-Kinases