The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Yeaman, Stephen J.; Cohen, Philip; Watson, David; Dixon, Gordon H.

doi:10.1042/bj1620411

Cited by 144 publications

(27 citation statements)

References 30 publications

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“…Thus, addition of the second arginine is a strong negative determinant for CaM-kinase II. This is of particular interest since addition of the second arginine is a strong positive determinant for cAMP-kinase [47,48].…”

Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

Calcium/Calmodulin-Dependent Protein Kinase II

Colbran

Soderling

1990

Current Topics in Cellular Regulation

173

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Section: Species Tissue and Subcellular Distributionmentioning

confidence: 99%

Calcium/Calmodulin-Dependent Protein Kinase II

Colbran

Soderling

1990

Current Topics in Cellular Regulation

173

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“…Cyclic AMP-dependent protein kinase has been shown to phosphorylate one serine residue on the a-subunit and one serine residue on the P-subunit of phosphorylase kinase [23,24]. The tryptic phosphopeptide from the a-subunit (40 amino acids) is much larger than that from the /Ssubunit (9 amino acids) and the two sites are therefore easily distinguished by gel filtration [23].…”

Section: 1 Phospho~~a~~n Of Phospho~~se Kinase By Cyclic Amp and mentioning

confidence: 99%

Phosphorylation of rabbit skeletal muscle phosphorylase kinase by cyclic GMP‐dependent protein kinase

Cohen

1980

FEBS Letters

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“…This hypothesis is in agreement with the suggestion of Ribadeau-Dumas and coworkers who have pointed out [I51 that all the phosphate residues in casein are located two residues on the amino-terminal side of, either a glutamyl or another phosphoseryl residue. Accumulated evidence on the specificity of the mammalian cyclic-AMP-dependent protein kinase indicates that it also recognises amino acid sequences rather than three-dimensional conformations [19,20]. In that case the requirement is for two adjacent basic residues situated on the amino side of a susceptible seryl or threonyl residue.…”

Section: Discussionmentioning

confidence: 99%

Specific Casein Phosphorylation by a Casein Kinase from Lactating Bovine Mammary Gland

Mackinlay

West

Manson

1977

European Journal of Biochemistry

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1. A preparation which contains protein kinase activity capable of rephosphorylating dephosphorylated @,I and P-caseins has been prepared from lactating bovine mammary gland. This activity is localised in the Golgi fraction and in this respect is similar to that obtained previously from rat tissue. It differs from the rat preparation in being unable to rephosphorylate dephosphorylated x-casein.2. Progressive dephosphorylation of asl and P-caseins increases the rate of their rephosphorylation in the presence both of Ca2+ and of Mg2+. For 8-casein significant non-specific phosphorylation occurs in the presence of Mg2+ while in the presence of Ca2+ the level of phosphorylation is very low.3. Comparison of the products of the action of this kinase on partially dephosphorylated aSl and B-caseins indicates that seryl residues grouped with pre-existing phosphoseryl residues are phosphorylated preferentially in the presence of Mg2 +, while the phosphorylation of isolated single seryl residues is promoted by Ca2+.4. Digests of aSl-casein, prepared by treatment with cyanogen bromide, have been fractionated and the three major peptides, separated. After dephosphorylation two of these, which between them contain all of the phosphate of aS1-casein, are rephosphorylated at sites occupied in the native protein by phosphoseryl residues, i. e., at positions 46, 48, 75 and 115 of the a,l-casein molecule. Evidence is presented which shows that this specificity of action also operates when intact aSl-casein is used as phosphate acceptor. It is concluded that the enzyme responsible for specific phosphorylation acts through recognition of an amino acid sequence and does not require the provision of a specific structural conformation in the protein substrate.Determination of the sequences of amino acid residues occurring in the three major components of bovine casein, @,I, P and x-caseins, has defined accurately the locations of the phosphate residues in these proteins [1,2]. Altogether some 14 seryl residues are phosphorylated and a prominent feature of the primary structures of the a ,~ and p-caseins is a region of homology which includes a cluster of four phosphoseryl residues. In aSl-casein this extends over residues 63 -70 thus : Glu-Ser(P)-Ile-Ser(P)-Ser(P)-Ser-(P)-Glu-Glu, a sequence which is repeated in residues 14-21 of /?-casein with the substitution of leucine for isoleucine. In addition to these a,l-casein contains four phosphoseryl residues located at positions 46, 48, 75 and 11 5 and P-casein contains one located at position 35. %-Casein contains only one phosphoseryl residue. It has been shown by Turkington and Topper [3] that in mouse mammary glands at least a significant proportion of the phosphate of casein is incorporated after polypeptide synthesis rather than by incorporation of phosphorylated amino acids, and more recently Bingham and coworkers [4,5] have detected in the Golgi apparatus of lactating rat mammary gland a protein kinase for which dephosphorylated bovine caseins were found to act as better phosphat...

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The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

Cited by 144 publications

References 30 publications

Calcium/Calmodulin-Dependent Protein Kinase II

Calcium/Calmodulin-Dependent Protein Kinase II

Phosphorylation of rabbit skeletal muscle phosphorylase kinase by cyclic GMP‐dependent protein kinase

Specific Casein Phosphorylation by a Casein Kinase from Lactating Bovine Mammary Gland

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