Shepherd, PR; Withers, DJ; Siddle, K; (1998) Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling. BIOCHEM J , 333 471 - 490.
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Insulin plays a key role in regulating a wide range of cellular processes. However, until recently little was known about the signalling pathways that are involved in linking the insulin receptor with downstream responses. It is now apparent that the activation of class la phosphoinositide 3-kinase (PI 3-kinase) is necessary and in some cases sufficient to elicit many of insulin's effects on glucose and lipid metabolism. The lipid products of PI 3-kinase act as both membrane anchors and allosteric regulators, serving to localize and activate downstream enzymes and their protein substrates. One of the major ways these lipid products of PI 3-kinase act in insulin signalling is by binding to pleckstrin homology (PH) domains of phosphoinositide-dependent protein kinase (PDK) and protein kinase B (PKB) and in the process regulating the phosphorylation of PKB by PDR. Using mechanisms such as this, PI 3-kinase is able to act as a molecular switch to regulate the activity of serine/threonine-specific kinase cascades important in mediating insulin's effects on endpoint responses.
|Title:||Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling|
|Keywords:||PROTEIN-KINASE-B, GLYCOGEN-SYNTHASE KINASE-3, RAT SKELETAL-MUSCLE, P70 S6 KINASE, GROWTH-FACTOR-I, STIMULATED GLUCOSE-TRANSPORT, PLECKSTRIN HOMOLOGY DOMAINS, RECEPTOR SUBSTRATE-1 IRS-1, GTPASE-ACTIVATING PROTEIN, ACTIVE PHOSPHATIDYLINOSITOL 3-KINASE|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology|
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences > Medicine (Division of)
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