BIOC 4520 Study Guide - Midterm Guide: Phosphoenolpyruvate Carboxykinase, Insulin Receptor Substrate, Sh2 Domain

• School: University of Guelph
• Department: Biochemistry
• Course: BIOC 4520
• Professor: Manfred Brauer

Document Summary

Insulin in blood binds with insulin receptor [insulin binding domain of the active insulin receptor protein (ins-r) subunits on cell surface] Note: ins-r is an ( )2 dimer with subunits on cell surface and subunits traversing the membrane and protruding on the cytoplasm side of the membrane. Binding of insulin to subunit causes conformational change in subunits which then auto-pylate the tyrosine residues of the other subunit (tyrosine kinase activity. Insulin receptor substrate 1 (irs1) binds to the newly accessible substrate binding domain of ins-r, and is phosphorylated (activated) at a tyrosine residue. Note: irs-1 has a number of pathways that it is involved in. Phosphoinositide 3-kinase (pi-3k) binds irs-1 at its sh2 domain and becomes activated. Pi-3k proceeds to phosphorylate phosphotidylinotisol 4,5-biphosphate (pi-p2) to. Pi-p3 binds phosphotidyl-inotisol dependent kinase (pdk), which is then activated. Pi-p3 also binds protein kinase b (pkb or akt), which is then pylated and activated by.