BIO 211 Lecture Notes - Lecture 6: Map Kinase Kinase Kinase, Phosphatidylinositol (3,4,5)-Trisphosphate, Lipid Signaling

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Enzyme-coupled receptors- transmembrane proteins with their ligand binding domain on the outer surface of the plasma membrane. Receptor tyrosine kinases (rtks)- secreted and cell-surface-bound proteins that control cell behavior in both developing and adult animals. Signal protein binds to ligand-binding domain on the extracellular side of the receptor. Allows the two cytoplasmic kinase domains to come together to become activated: not all kinases are activated by this method (phosphorylation) Some require conformational changes caused by the interactions between 2 kinase domains: gpcrs are believed to change orientation when bound to a ligand. Phosphorylated tyrosines on rtks serve as docking sites for intracellular signaling. Additional docking proteins can be used to enlarge the complex. Proteins with sh2 domains bind to phosphorylated tyrosines: many intracellular signaling proteins can bind to the phosphotyrosine on activated rtks, help relay the signal through protein-protein interactions, mediated by interaction domains. Phospholipase c-gamma (plcgamma)- responsible for activating the inositol phospholipid signaling pathway.

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