Titlebook: Cellular Regulation by Protein Phosphorylation; Ludwig M. G. Heilmeyer Conference proceedings 1991 Springer-Verlag Berlin Heidelberg 1991

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Identification of Phosphorylation Sites in the Nicotinic Acetylcholine Receptor by Edman Degradationis α.β.δ with the α-subunits containing the binding sites for cholinergic agonists and antagonists. Signal transduction occurs upon opening of an ion channel by agonist binding. This channel has been identified as being formed by homologous helical sequences contributed by the subunits (Helix M2 mod

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A Sensitive Colorimetric Assay for Protein Phosphatase Activityalyze the addition to, and phosphatases the removal of phosphate groups from serine, threonine, tyrosine and other amino acid residues (Boyer & Krebs, 1986). We present here a simple and sensitive colorimetric assay for protein phosphatase activity based on the determination of released Pi by an imp

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Protein Kinase Structure & Function: cAMP-Dependent Protein Kinaseenzymes. Nearly all major metabolic pathways are regulated at some step by phosphorylation. In addition, protein kinases play critical roles in mitogenesis, in cell cycle events, and in many types of oncogenesis. One of the first protein kinases to be discovered was cAMP-dependent protein kinase (cA

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Expression in , of Mutated R Subunits of the cAMP-Dependent Protein Kinase from ,.mutagenesis was used to introduce single amino-acid substitutions in either cAMP binding site A (Gly to Glu at position 135) or site B (Gly to Glu at position 261). Analysis of the mutated R subunits showed that both single mutants retain high affinity cAMP binding activity (Kd = 20 nM) while cAMP d

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Conformational and Shape Changes Associated with cAMP- Dependent Protein Kinaseically of the protein kinases (Taylor et al., 1990). cAPK is composed of both regulatory (R) and catalytic (C) subunits. In the absence of cAMP the subunits associate with a high affinity to form an inactive tetrameric (R.C.) holoenzyme. cAMP binds to the R-subunit promoting the dissociation of the

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Crystallographic Studies of the Catalytic Subunit of cAMP- Dependent Protein Kinaseo regulatory and two catalytic (C) subunits. Upon binding cAMP the regulatory dimer releases two monomeric C-subunits, which then use MgATP to phosphorylate serine or threonine residues found typically in the sequence Arg-Arg-X-Ser/Thr in target proteins. Protein phosphorylation is a well-known mech

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