Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.1 (protein kinase)
 81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Rel-associated protein pp40 is functionally related to I kappa B, an inhibitor of the transcription factor NF-kappa B. Purified pp40 inhibits the DNA binding activity of the NF-kappa B protein complex (p50:p65 heterodimers), p50:c-Rel heteromers, and c-Rel homodimers. The sequence of the complementary DNA encoding pp40 revealed similarity to the gene encoding MAD-3, a protein with mammalian I kappa B-like activity. Protein sequencing of I kappa B purified from rabbit lung confirmed that MAD-3 encodes a protein similar to I kappa B. The sequence similarity between MAD-3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin. These results suggest that rel-related transcription factors, which are capable of cytosolic to nuclear translocation, may be held in the cytosol by interaction with related cytoplasmic anchor molecules.
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PMID:Rel-associated pp40: an inhibitor of the rel family of transcription factors. 189 14

The relationship and substrate specificity of the human erythrocyte membrane kinase and casein kinase A were investigated. Based on Staphylococcus aureus V8 protease digestion patterns, the 2 kinases appeared to be structurally homologous. These enzymes also exhibited the same substrate specificity and phosphorylated the same synthetic peptides and domains of ankyrin. Both kinases did not utilize GTP effectively as a substrate and were not inhibited by low concentrations of heparin, suggesting that they were type I casein kinases. An analysis of synthetic peptide phosphorylation failed to reveal a specific pattern of recognition of the amino acid sequence surrounding the phosphorylation site.
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PMID:Identity and substrate specificity of human erythrocyte membrane-bound and cytosolic casein kinases. 195 95

1. In whole ghosts, ankyrin, protein 4.1, protein band 3 and spectrin are lysed by purified calpain I in the presence of calcium. 2. Limited calpain lysis of purified ankyrin results in several peptides, including a 85 kD peptide bearing the ankyrin interaction site for the protein band 3 internal fragment (43 kD), and a 55 kD peptide carrying the ankyrin-spectrin interaction site. 3. These peptides are differently phosphorylated: the 85 kD by cytosol casein kinase, and the 55 kD by membrane casein kinase. 4. Protein 4.1 lysis mainly produces a 30 kD peptide resistant to proteolysis. 5. The spectrin beta-chain is more sensitive to calpain cleavage than the alpha chain; both chains seem to be cleaved in a similar sequential manner. 6. Limited proteolysis of spectrin dimer does not impede tetramerization in vitro.
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PMID:In vitro digestion of spectrin, protein 4.1 and ankyrin by erythrocyte calcium dependent neutral protease (calpain I). 214 14

The effects of phosphorylation on the interaction between spectrin and ankyrin were investigated. Spectrin and ankyrin were phosphorylated using purified human erythrocyte membrane and cytosolic (casein kinase A) kinases. These two kinases have similar properties as well as activities toward spectrin and ankyrin. Both kinases catalyzed the incorporation of about 2 mol of phosphate/mol of spectrin and about 7 mol of phosphate/mol of ankyrin. These phosphates were incorporated primarily into seryl and threonyl residues of the proteins. The phosphopeptide maps of ankyrin phosphorylated by the membrane kinase and casein kinase A were identical. Binding studies indicate that ankyrin exhibits different affinities for spectrin dimers (KD = 2.5 +/- 0.9 X 10(-6) M) and tetramers (KD = 2.7 +/- 0.8 X 10(-7) M). These dissociation constants were not appreciably affected by the phosphorylation of spectrin. On the other hand, phosphorylation of ankyrin was found to significantly reduce its affinity for either phosphorylated or unphosphorylated spectrin tetramers (KD = 1.2 +/- 0.1 X 10(-6) M) but not spectrin dimers (KD = 2.5 +/- 0.4 X 10(-6) M). The same results were obtained using either the membrane kinase or casein kinase A as the phosphorylating enzyme. The above observation suggests that ankyrin phosphorylation may provide an important mechanism for the regulation of the erythrocyte membrane cytoskeletal network.
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PMID:Phosphorylation of ankyrin decreases its affinity for spectrin tetramer. 293 95

An improved method for purifying erythrocyte band 4.1, the protein which mediates the interaction between spectrin and actin, has been developed. The new procedure, using adsorption chromatography on hydroxylapatite crystals immobilized within a crosslinked agarose gel (HA-Ultrogel), is simple and reproducibly provides a high yield of band 4.1 which is essentially free of protein kinase. Other components eluted from the hydroxylapatite matrix include band 4.9, ankyrin, and a 35,000-Da polypeptide that appears to be glyceraldehyde-3-phosphate dehydrogenase that remains bound to the erythrocyte membrane in 150 mM NaCl.
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PMID:Purification of erythrocyte band 4.1 and other cytoskeletal components using hydroxyapatite-Ultrogel. 294 Sep 39

Novel polypeptides with Mr values about 140,000 bind fodrin and spectrin and are enriched in the postsynaptic density (PSD) compared to other tissues or subcellular fractions. 125I-fodrin binding to these polypeptides is competed for by unlabeled spectrin. These polypeptides are distinct from ankyrin and its proteolytic fragments and from band 4.1 which also bind fodrin. Phosphorylation of PSDs by the endogenous calmodulin-dependent protein kinase markedly reduces 125I-fodrin binding to the transblotted preparation. Such an event may play a regulatory role in governing protein-protein interactions among elements of the PSD.
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PMID:Involvement of fodrin-binding proteins in the structure of the neuronal postsynaptic density and regulation by phosphorylation. 294 77

Human erythrocyte casein kinase A, previously identified as a seryl, threonyl kinase, was found also to catalyze the phosphorylation of protein tyrosine. Phosphorylation of tyrosyl residues was detected in angiotensin-II and in several tyrosine containing synthetic peptides. In addition, phosphorylation on tyrosyl residues was also observed in alkylated bovine serum albumin and in band 3 and ankyrin purified from human erythrocyte membranes. The identification of phosphotyrosine was conducted using two-dimensional thin layer electrophoresis at pH 1.9 and 3.5 after acid hydrolysis of the phosphoproteins. It should be noted, however, that the major phosphorylation sites in band 3 and ankyrin catalyzed by casein kinase A were seryl and threonyl residues.
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PMID:Phosphorylation of protein tyrosine by human erythrocyte casein kinase A. 294 63

The phosphorylation of the cytoplasmic domain of band 3 by the human erythrocyte membrane kinase and casein kinase A has been investigated. The cytoplasmic domain of band 3 was released from erythrocyte vesicles by treatment with alpha-chymotrypsin and isolated as a 43,000-Da peptide. Both the membrane kinase and casein kinase A catalyzed the incorporation of about 1 mol of phosphate per mole of the band 3 fragment. The phosphorylation of the band 3 fragment by both kinases was not additive, suggesting that the two enzymes might recognize the same phosphorylation sites. Also in support of this notion was the observation that the phosphopeptide maps of the band 3 fragment phosphorylated by the two kinases were identical. Phosphoamino acid analysis of the band 3 fragment phosphorylated by casein kinase A revealed the presence of approximately equal amounts of phosphoserine and phosphothreonine and, to a lesser extent, phosphotyrosine. The interaction between the 43,000-Da peptide with ankyrin and the effect of phosphorylation on this interaction have been examined. The band 3 fragment was found to form two different types of complexes, termed C1 and C2, with ankyrin in a saturable manner. The C1 and C2 complexes contained about 1.7 and 0.43 mol of band 3 fragment per mole of ankyrin, respectively. Interestingly, these binding stoichiometries were found to be reduced by half by the phosphorylation of ankyrin but not by the phosphorylation of the band 3 fragment. The results suggest that the structure and dynamics of the erythrocyte membrane cytoskeletal network may be regulated by phosphorylation.
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PMID:Analysis of band 3 cytoplasmic domain phosphorylation and association with ankyrin. 295 9

In contrast to the properties of spectrin obtained from [32P]phosphate-labeled red cells, purified spectrin dimer could be phosphorylated by a cAMP-dependent protein kinase from bovine heart. Both spectrin bands were phosphorylated. Spectrin band 2 contained in addition to autophosphorylated peptides several phosphopeptides that were distinct from autophosphorylated ones. The cAMP-dependent phosphorylation of spectrin band I was modulated by reducing agent and the concentration of spectrin. At high concentrations spectrin band 2 was predominantly labeled. The cAMP-dependent phosphoform of spectrin band 2 had a pI slightly higher than that of autophosphorylated spectrin band 2, but lower than that of ankyrin.
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PMID:A cyclic AMP-dependent phosphorylation of spectrin dimer. 671 31

The sequence of RNase L has been re-examined by computer analysis. We propose a molecular architecture of RNase L, with an unusual combination, in one protein chain, of 9 ankyrin-like repeats, a functional active protein kinase and a C-terminal catalytic RNase similar to the yeast protein, IRE1. The protein kinase may be involved in a new signal transduction pathway which remains to be discovered.
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PMID:A hybrid protein kinase-RNase in an interferon-induced pathway? 769 13


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