BIOMG 1350 Lecture Notes - Lecture 15: Glycogen Phosphorylase, Phosphorylase Kinase, Lipid Signaling
Document Summary
G-protein coupled receptors (gpcrs) largest family of cell surface receptors (>700: 7 pass transmembrane proteins, wide variety of signaling molecules that can activate, ~1/3 drugs used today act through gpcrs. Gpcrs activate g proteins: trimeric g proteins (3 subunits) Beta, gamma covalently attached lipid tails to membrane. Alpha bound to gdp: signal molecule interacts with gpcr, gpcr changes conformation on cytosolic side of protein. Site for bonding for g protein: activated receptor acts as a gef for its g protein. Gdp associated from alpha: alpha will then bind gtp activated. Releases from receptor and dissociates from beta-gamma subunit. Can stay together, depends on type of g-protein: effector activation. Receptor can activate many molecules of g protein. G protein alpha subunit switches itself off: signal molecule stops being sent, hydrolysis of gtp by subunit inactivates subunit within seconds (helped by rgs) Goes back to gpcr to get reactivated (gdp displacement, gtp bind: causes it to dissociate from target protein.