Polycation‐dependent, Ca2+‐antagonized phosphorylation of calmodulin by casein kinase‐2 and a spleen tyrosine protein kinase

  title={Polycation‐dependent, Ca2+‐antagonized phosphorylation of calmodulin by casein kinase‐2 and a spleen tyrosine protein kinase},
  author={Flavio Meggio and Anna Maria Brunati and Lorenzo A. Pinna},
  journal={FEBS Letters},
Ten distinct protein kinases have been tested for their ability to phosphorylate calmodulin. Only casein kinase‐2 and a spleen tyrosine protein kinase (TPK‐III) proved effective, their phosphorylation efficiency being dramatically enhanced by histones and other polybasic peptides while being depressed by 50 μM Ca2+. Phosphorylation by CK‐2 takes place with a Km of 12 μM calmodulin, leading to the incorporation of more than 1.5 mol P/mol substrate. Ser81 and Thr79 are among the residues affected… Expand
Tyrosine phosphorylation modulates the interaction of calmodulin with its target proteins.
Direct determination by fluorescence techniques of the dissociation constants with synthetic peptides corresponding to the CaM-binding domain of the six analysed enzymes revealed that phosphorylation of Tyr99 on CaM generally increased its affinity for the peptides. Expand
Phosphorylation of calmodulin. Functional implications.
The description of the phosphorylation events mediated by the different protein kinases not only in the test tube but in intact cells will be emphasized, theosphorylation-mediated changes of CaM activity, its action on CaM-dependent systems, and the functional repercussion of these phosphorylated processes in the physiology of the cell are summarized. Expand
Phosphorylation of calmodulin
Calmodulin (CaM) is phosphorylated in vitro and in vivo by multiple protein-serine/threonine and protein-tyrosine kinases. Casein kinase II and myosin light-chain kinase are two of the wellExpand
Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase.
An epidermal-growth-factor(EGF)-receptor preparation isolated from rat liver plasma membranes is able to phosphorylate calmodulin, which was enhanced 3-8-fold by EGF and inhibited by micromolar concentrations of Ca2+. Expand
Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV.
CaM-kinase IV activated by binding Ca2+/CaM can bind and phosphorylate another CaM with the aid of poly(Lys, leading to a decrease in the activity of CaM. Expand
Substrate recognition by casein kinase‐II: The role of histidine‐160
Results show that H160 is not primarily involved in canonical substrate recognition, but does interact with an acidic residue located at position −2 with respect to the target Ser/Thr, which is important for interaction of substrates with the enzyme. Expand
Stimulation of Ca(2+)/calmodulin-dependent protein kinase phosphatase by polycations.
The Glu cluster appeared to be the binding site for polycations and to play a pivotal role in the polycation stimulation of CaMKPase activity. Expand
Phosphorylation of calmodulin on threonine residue(s) by cytosol prepared from the adrenal cortex.
  • M. Kubo, C. Strott
  • Biology, Medicine
  • Biochemical and biophysical research communications
  • 1988
During the course of experiments examining Ca2+/calmodulin-dependent protein phosphorylation by cytosol prepared from the outer and inner zones of the guinea pig adrenal cortex, it appeared that theExpand
Phosphorylation of Calmodulin by Permeabilized Fibroblasts Overexpressing the Human Epidermal Growth Factor Receptor
Detergent-permeabilized EGFR-T17 fibroblasts, which overexpress the human epidermal growth factor (EGF) receptor, phosphorylate both poly-L-(glutamic acid, tyrosine) and exogenous calmodulin in anExpand
Effect of poly-basic amino acids on the phosphorylation of various substrate proteins by cytosolic protein-tyrosine kinase from porcine spleen.
Effect of poly-basic amino acids on CPTK-40 seems to be mainly on the substrate proteins, rather than on the enzyme itself, but polyarginine and polyornithine have similar effects on this phosphorylation reaction. Expand


Discovery of A Ca2+‐and calmodulin‐dependent protein phosphatase
The serine residue on the a-sub unit, as well as that on the@subunit, becomes phosphorylated in vivo in response to adrenaline, suggesting that it may have a physiological function. Expand
Distinct structural requirements of Ca2+/phospholipid‐dependent protein kinase (protein kinase C) and cAMP‐dependent protein kinase as evidenced by synthetic peptide substrates
It is concluded that, while both protein kinase C and A‐kinase need basic groups close to the phosphorylatable residues, their primary structure determinants are quite distinct. Expand
Phosphorylation of tyrosine residues of calmodulin in Rous sarcoma virus-transformed cells.
It is inferred that Ca2+ may regulate the level of tyrosine phosphorylation of calmodulin in RSV-transformed cells, and phosphorylated in turn may attenuate the function of this protein in vivo. Expand
Isolation and partial characterization of distinct forms of tyrosine protein kinases from rat spleen
Three peaks of tyrosine protein kinase activity can be resolved when the extract of rat spleen particulate fraction is subjected to DEAE‐cellulose gradient chromatography. Expand
Site specificity of casein kinase-2 (TS) from rat liver cytosol. A study with model peptide substrates.
The factors determining the site recognition and phosphorylation by rat liver casein kinase-2 (CK-2) have been explored with a set of 14 related hexapeptides each including a single phosphorylatable amino acid and five acidic plus neutral residues, and their kinetic and inhibition constants were determined. Expand
The amino acid sequence of the delta subunit (calmodulin) of rabbit skeletal muscle phosphorylase kinase.
The amino acid sequence of the phosphorylase kinase delta subunit has been determined using cyanogen bromide peptides and the sequences of the N-terminal tripeptide and the amide assignments on residues 58 and 60 were not determined unequivocally. Expand
Structure and properties of casein kinase-2 from Saccharomyces cerevisiae. A comparison with the liver enzyme.
It is suggested that the beta subunit of animal CK-2 may play a role in determining both the stability of the enzyme and its regulation and that, consequently, the different properties of YCK- 2 may be at least in part accounted for by its lack of beta subunits. Expand
The protein phosphatases involved in cellular regulation
Spermine increased the activity of protein phosphatase-2A towards eight of nine substrates tested and was a more potent activator than spermidine, while putrescine had only a small effect, and Mn2+ could not mimic the activating effect of spermine on dephosphorylation of glycogen synthase (labelled in sites-3) by protein phosph atase 1. Expand
Ca2+-dependent hydrophobic-interaction chromatography. Isolation of a novel Ca2+-binding protein and protein kinase C from bovine brain.
Several bovine brain proteins have been found to interact with a hydrophobic chromatography resin (phenyl-Sepharose CL-4B) in a Ca2-dependent manner and a novel Ca2+-binding protein that has now been purified to electrophoretic homogeneity is found. Expand
Structural similarities between the Ca2+-dependent regulatory proteins of 3':5'-cyclic nucleotide phosphodiesterase and actomyosin ATPase.
Results of studies of the Ca2+-dependent protein modulator of 3':5'-cyclic nucleotide phosphodiesterase isolated from bovine brain are presented which show its structural similarity to theExpand