BIOC 311 Lecture Notes - Lecture 29: Insulin Receptor Substrate, Glycogen Synthase, Insulin Receptor
12 Feb 2020
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Interacts with cytosolic kinases, which then interacts with gene-regulating proteins (usually through activation) Specificity: one ligand, one receptor (note: one hormone can have many receptors, you just can"t have many hormones for one receptor) Desensitization/adaptation: activation of a negative feedback signal. 1 tm domain, with cytosolic and ecs portion. They have a tyrosine kinase activity, majority need to dimerize and transphosphorylate in order to function. We will be seeing the insulin receptor as a prototype for this class of receptor. Subunits are bound through sulfide bond. Change of conformation upon binding activation of tyrk, transphosphorylation, recruitment of insulin receptor substrate via sh2. Insulin binds to receptor: activates glycogen synthase, stimulates recruitment of glut4, activation of trk, adds phosphate pi3k, which converts pip2 pip3, pip3 recognized by pdk1 and pdk2, activate pkb to inhibit gsk3, gsk stops inhibiting glycogen synthase, via pip3. Recruitment of glut4 in adipose tissue and muscle.
