P proteins on tyrosine residues less than 1 dual

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P proteins on tyrosine residues (less than 1%) “dual-function” kinases can P all 3 In all cases, the kinases transfer the terminal P from ATP to the hydroxyl moiety of the given amino acid Requires Mg2+ P’lation changes the charge of the protein substrate alters conformation alters function
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Schema of phosphorylation
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Ser-Thr Kinases The most well-investigated protein kinases in the brain are those stimulated by cAMP, cGMP, Ca2+ and DAG
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cAMP-dependent kinases (PKA) cAMP (stimulated upon Gs-signaling ) binds to regulatory subunits of PKA and causes their dissociation from the catalytic subunits PKA is high compartmentalized but associated with PM, cytoplasm and nucleus Anchored by A kinase Anchor Proteins (AKAPs) , which bind to the regulatory subunits (keep the protein kinase in close proximity to signal transduction molecules that it P’lates) cGMP-dependent kinases (PKG) cGMP binds to the regulatory domain of PKG but the kinase does not dissociate more limited range of function Has a more restricted expression pattern than PKA smaller number of 2 nd messenger actions Protein Kinase C Activated by Ca2+, in conjunction with DAG (but depends on the isozyme; “conventional” require both; “novel” are Ca-independent) Activation tends to move kinase from cytoplasm to the PM When activated, PKC binds to RACKs (receptors for activated C kinase) , which are aligned in series at the plasma membrane and bring PKC closer to substrates)
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