Phosphorylase kinase phosphorylation of skeletal-muscle troponin T

Risnik, Vladimir V.; Добровольский, А. Б.; Gusev, Nikolai B.; Severin, S E

doi:10.1042/bj1910851

Cited by 14 publications

(8 citation statements)

References 27 publications

(35 reference statements)

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“…Glycogen synthase kinase-5 [2] is identical to an enzyme that has a ubiquitous tissue distribution, and has been variously termed casein kinase TS [ 191,, casein kinase-G [21], casein kinase N-II [22] and troponin-T kinase [23,24]. Several physiological substrates of this enzyme have been identified including glycogen synthase [6,7], the Rn-subunit of cyclic AMPdependent protein kinase [25,26] and troponin-T [24,27] in muscle, and the,&subunit of protein synthesis initiation factor eIF-2 in reticulocytes [28,29].…”

Section: Discussionmentioning

confidence: 99%

“…Effect of phosphorylation by cyclic AMPdependent protein kinase (triangles) or phosphorylase kinase (circles) on the rate of phosphorylation of glycogen synthase by glycogen synthase kinase-3. Glycogen synthase was phosphorylated with the catalytic subunit of cyclic AMP-dependent protein kinase (lOU/ml) to 2.15mol/mol subunit [site la = 0.7, site lb = 0.65, site 2 = 0.8mol/mol subunit [23] or with phosphorylase kinase (lOpg/ml) to 0.45 mol/mol subunit, using the phosphorylation assay described in section 2.2. except that unlabelled ATP was used. The phosphorylation stoichiometries were established by separate parallel incubations with [y-32P]ATP.…”

Section: 5mentioning

confidence: 99%

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Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle

et al. 1982

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Glycogen synthase kinase-5 (casein kinase-II) phosphorylates glycogen synthase on a serine termed site 5. This residue is just C-terminal to the 3 serines phosphorylated by glycogen synthase kinase-3, which are critical for the hormonal regulation of glycogen synthase in vivo. Although phosphorylation of site 5 does not affect the catalytic activity, it is demonstrated that this modification is a prerequisite for phosphorylation by glycogen synthase kinase-3. Since site 5 is almost fully phosphorylated in vivo under all conditions, the role of glycogen synthase kinase-5 would appear to be a novel one in forming the recognition site for another protein kinase

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Section: Discussionmentioning

confidence: 99%

Section: 5mentioning

confidence: 99%

Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle

et al. 1982

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“…3). Others Perry, 1980;Risnik et al, 1980;Pinna et al, 1981) have reported that serine in skeletal and cardiac troponin I and troponin T is the major site of phosphorylation by other protein kinases. It appears therefore that the Ca2+-dependent enzyme had a greater phosphorylation capacity and that threonine was specifically phosphorylated by this enzyme.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of skeletal-muscle troponin I and troponin T by phospholipid-sensitive Ca2+-dependent protein kinase and its inhibition by troponin C and tropomyosin

Mazzei¹,

Kuo²

1984

Biochemical Journal

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Skeletal-muscle troponin I and troponin T were found to be rapidly phosphorylated by cardiac phospholipid-sensitive Ca2+-dependent protein kinase, with Km values of 6.66 and 0.13 microM respectively. Stoichiometric phosphorylation of skeletal troponin I (endogenous phosphate content 0.7 mol/mol) indicated that the Ca2+-dependent enzyme and cyclic AMP-dependent protein kinase incorporated 0.9 and 0.8 mol/mol respectively. The same experiments with skeletal troponin T (endogenous phosphate content 1.9 mol/mol) revealed a maximal phosphorylation of 2 mol/mol by the Ca2+-dependent enzyme, whereas the cyclic AMP-dependent enzyme was unable to phosphorylate troponin T. The Ca2+-dependent enzyme phosphorylated both serine and threonine residues in skeletal and cardiac troponin I or troponin T; the cyclic AMP-dependent enzyme, in comparison, phosphorylated only serine in skeletal and cardiac troponin I. Although an equimolar amount of skeletal or cardiac troponin C markedly inhibited (80-90%) phosphorylation of skeletal and cardiac troponin I by the Ca2+-dependent enzyme, these troponin C preparations inhibited only phosphorylation of skeletal troponin I, but not that of cardiac troponin I, by the cyclic AMP-dependent enzyme. Calmodulin and Ca2+-binding protein S-100a could mimic the inhibitory effect of troponin C. A tissue specificity appeared to exist for the skeletal troponin T-skeletal troponin C interaction. Inhibition of troponin T phosphorylation by an equimolar amount of troponin C was lower than that of troponin I phosphorylation; these findings might explain in part why troponin T was the major substrate for the Ca2+-dependent enzyme in the troponin complex. The present studies indicate that skeletal and cardiac troponin I and troponin T were effective substrates for phospholipid-sensitive Ca2+-dependent protein kinase, suggesting a potential involvement of this Ca2+-effector enzyme in the regulation of myofibrillar activity.

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“…Glycogen synthase [22], the R I I subunit [37] and troponin-T [39,44], as normally isolated, contain substantial amounts of phosphate in the site(s) phosphorylated by glycogen synthase kinase 5 even though no precautions are taken to prevent the action of endogenous protein phosphatases during the preparation. This suggests that these sites may be rather poor substrates for protein phosphatases in mammalian muscle.…”

Section: Discussionmentioning

confidence: 99%

“…90% of the alkali-labile phosphate in the R I I subunit, as normally isolated, is located in the thermolytic peptide containing serine-74 and serine-76, indicating that glycogen synthase kinase 5 phosphorylates the Rlr subunit in vivo. Glycogen synthase kinase 5 [14] is identical to an enzyme that has a ubiquitous tissue distribution, and has been variously termed casein kinase TS [33], casein kinase I1 1341, casein kinase G [35], casein kinase N-I1 [36] and troponin-T kinase [37,38]. The R I I subunit is the third physiological substrate of this enzyme to be identified in mammalian muscle, the other two being glycogen synthase [22] and troponin-T [38, 391.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of the Type‐II Regulatory Subunit of Cyclic‐AMP‐Dependent Protein Kinase by Glycogen Synthase Kinase 3 and Glycogen Synthase Kinase 5

Hemmings

Aitken

Cohen

et al. 1982

European Journal of Biochemistry

171

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The regulatory (RI,) subunit of type-I1 cyclic-AMP-dependent protein kinase from bovine heart is phosphorylated at a significant rate in vitro by glycogen synthase kinase 3 and glycogen synthase 5, but not by glycogen synthase kinase 4 or phosphorylase kinase. The regulatory (RI) subunit of type-I cyclic-AMP-dependent protein kinase from rabbit skeletal muscle is not phosphorylated by any of these four protein kinases.Glycogen synthase kinase 3 phosphorylates two serine residues on the R~I subunit located 44 and 47 amino acids from the N terminus of the polypeptide chain. Glycogen synthase kinase 5 phosphorylates serine-74 and serine-76. These sites are distinct from the residue phosphorylated by the catalytic subunit of cyclic-AMPdependent protein kinase (serine-95).The Rll subunit, as normally isolated, contains 1.5-1.8 mol alkali-labile phosphate per subunit. At least 80 % of this phosphate (z 1.3 mol/subunit) is located in the thermolytic peptide containing serine-74 and serine-76, demonstrating that phosphorylation of the RII subunit by glycogen synthase kinase 5 occurs in vivo.Only small amounts of phosphate (z 0.1 mol/subunit) are associated with the thermolytic peptides containing serine-44/serine-47 and serine-95. The phosphorylation sites on the RIr subunit are organised in a strikingly similar manner to those of glycogen synthase, the amino acid sequences in the immediate vicinity of the phosphorylation sites showing a particular resemblance. These include the presence of a number of proline residues near the sites phosphorylated by glycogen synthase kinase 3, five consecutive acidic residues C-terminal to the sites phosphorylated by glycogen synthase kinase 5, and two adjacent arginine residues just N-terminal to the sites phosphorylated by the catalytic subunit of cyclic-AMP-dependent protein kinase.Glycogen synthase kinase 5 is very similar or identical to the enzyme that has been variously termed casein kinase TS, casein kinase 2, casein kinase G, casein kinase N-I1 or troponin-T kinase. The biological role of this enzyme is reviewed.

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Phosphorylase kinase phosphorylation of skeletal-muscle troponin T

Abstract: Rabbit skeletal-muscle troponin T was phosphorylated by a standard preparation of phosphorylase kinase [Cohen (1973)

Cited by 14 publications

References 27 publications

Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle

Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle

Phosphorylation of skeletal-muscle troponin I and troponin T by phospholipid-sensitive Ca2+-dependent protein kinase and its inhibition by troponin C and tropomyosin

Phosphorylation of the Type‐II Regulatory Subunit of Cyclic‐AMP‐Dependent Protein Kinase by Glycogen Synthase Kinase 3 and Glycogen Synthase Kinase 5

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