Phosphorylation protein kinases

Newton AC (2003) Regulation of the ABC kinases by phosphorylation protein kinase C as a paradigm. Biochem 1370 361-371... 

Volume 201. Protein Phosphorylation (Part B Analysis of Protein Phosphorylation, Protein Kinase Inhibitors, and Protein Phosphatases)... 

Alvarez, A., Toro, R., Caceres, A., Maccioni, R.B., 1999, Inhibition of tau phosphorylating protein kinase cdk5 prevents (1 amyloid-induced neuronal death, FEBS Lett., 459, 421 126... 

Multiple phosphorylation. Protein kinase A activates muscle phosphorylase kinase by rapidly phosphorylating its P subunits. The a subunits of phosphorylase kinase are then slowly phosphorylated, which makes the a and P subunits susceptible to the action of protein phosphatase 1. What is the functional significance of the slow phosphorylation of a ... 

B. Under these conditions, cAMP levels would remain elevated. Phosphorylation of pyruvate kinase causes its inactivation. Phosphorylase kinase and phosphorylase are activated by phosphorylation. Protein kinase A is not regulated by phosphorylation. 

Westerhoff M, Faoro L, Loganathan S, et al. Immrmohisto-chemical (IHC) expression of c-Met receptor tyrosine kinase (c-Met) has prognostic significance and its activation is related to phosphorylated protein kinase Cff (p-PKC ff) in malignant mesothelioma (MM). Mod Pathol. 2008 21 353A. 

Thalhofer, H. P., Daum, G., Harris, B. G. and Hofer, H. W. (1988) Identification of two different phosphofructokinase-phosphorylating protein kinases from Ascaris suum muscle. J. Biol. Chem. 263 952-957. 

There is kinetic evidence (66-67) that the target of allosteric effectors is CPS.B. Since the CPS subdomains are functionally and structurally equivalent, we were curious as to whether CPS.A could be placed under allosteric control. To determine whether this occurs, a second chimeric molecule (R2) was constructed (21) in which the mammalian regulatory domain (B3) replaced the A3 subdomain in E. coli CPS.A (Figure 11). The control mechanisms (Figure 12) are nearly the same as that observed for the mammalian CAD. The chimera is inhibited by UTP and activated by PRPP although the affinity for the latter ligand is somewhat lower than in the native molecule. While chimera R1 was catalytically active, its aggregation made it a poor substrate for protein kinase A. The second chimera, R2 is monodisperse and can be readily phosphorylated. Protein kinase A abolishes UTP inhibition and reduces the affinity of the protein for PRPP, the same effect observed in CAD. 

Kiss, Z., E. Deli, P.R. Girard, G.R. Pettit, and J.F. Kuo Comparative Effects of Polymyxin B, Phorbol Ester and Bryostatin on Protein Phosphorylation, Protein Kinase C Translocation, Phospholipid Metabolism and Differentiation of HL60 Cells. Biochem. Biophys. Res. Comm. 146, 208 (1987). 

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