Isolation of cDNA clones for the catalytic gamma subunit of mouse muscle phosphorylase kinase: expression of mRNA in normal and mutant Phk mice.

Chamberlain, Jeffrey S.; vanTuinen, Peter; Reeves, A A; Philip, B.A.; Caskey, C. Thomas

doi:10.1073/pnas.84.9.2886

Cited by 50 publications

(24 citation statements)

References 35 publications

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“…The gamma-M proteins from rat, rabbit, and mouse have >93% identical amino acid sequences (8,9,13,14). Rabbit gamma-M has been the most extensively characterized and most discussion of the gamma subunit in this review is based on what has been learned with respect to that protein.…”

Section: The Gamma Subunitmentioning

confidence: 99%

Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure

Brushia

Walsh²

1999

Front Biosci

168

176

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Section: The Gamma Subunitmentioning

confidence: 99%

Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure

Brushia

Walsh²

1999

Front Biosci

168

176

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“…The subunit y carries catalytic activity (6) and is similar to other known protein kinases (7). The primary structures of these subunits have been determined, and cDNAs encoding the subunit y have been cloned (8)(9)(10). The two large subunits, a and X3, comprise 80%o of the total protein.…”

mentioning

confidence: 99%

cDNA cloning and complete primary structure of skeletal muscle phosphorylase kinase (alpha subunit).

Zander

Meyer

Hoffmann-Posorske

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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We have isolated and sequenced a cDNA encoding the a subunit of phosphorylase kinase from rabbit fast-twitch skeletal muscle. The cDNA molecule consists of 388 nucleotides of 5'-nontranslated sequence, the complete coding sequence of 3711 nucleotides, and 342 nucleotides of 3'-nontranslated sequence followed by a poly(dA) tract. It encodes a polypeptide of 1237 amino acids and a deduced molecular mass of 138,422 Da. Nearly half of the deduced amino acid sequence is confirmed by peptide sequencing. Seven positions of endogenously phosphorylated serine residues and autophosphorylation sites, identified by peptide sequencing, could be assigned. They cluster in a segment of only 60 amino acids. RNA blot hybridization analysis demonstrates a predominant RNA species of -4500 nucleotides and a less abundant RNA of 8700 nucleotides. (19,21,22), and rats (23). Defects of the muscular and of the hepatic form of the enzyme and X chromosomal as well as autosomal transmission are observed. The isolation of DNA sequences encoding the subunits of phosphorylase kinase would make it possible to characterize the molecular nature of these deficiencies and may improve clinical diagnosis and genetic counseling.To these ends, we have determined large parts of the peptide sequence of the a subunit of phosphorylase kinase from rabbit fast-twitch skeletal muscle. We have used these sequences to design oligonucleotide probes and to isolate and identify cDNA molecules encoding this subunit. Here, we present the nucleotide sequence of a nearly complete mRNA copy, and the complete primary structure of the a subunitA Phosphorylase kinase (ATP:phosphorylase-b phosphotransferase, EC 2.7.1.38) was the first regulatory protein kinase to be discovered (1) and the starting point for revealing, during the last three decades, reversible protein phosphorylation as an important control mechanism in eukaryotic cells. It is a large oligomeric enzyme (1.3 MDa) with the subunit structure (afOyS)4. In linking glycogen breakdown to both nervous and endocrine stimulation, the enzyme is regulated in a complex way by phosphorylation of various serine residues and by calcium (2-4). The subunit 8 is identical to calmodulin and confers Ca2+ sensitivity to the enzyme (5). The subunit y carries catalytic activity (6) and is similar to other known protein kinases (7). The primary structures of these subunits have been determined, and cDNAs encoding the subunit y have been cloned (8-10). The two large subunits, a and X3, comprise 80%o of the total protein. They carry all phosphorylation sites; furthermore, they have been implicated in catalytic function (4, 11) as well as binding of nucleotides (11, 12), calmodulin (13), and troponin (14). Only small partial amino acid sequences have been published from a and ,8. To provide a structural basis for the wealth of enzymological data that has been accumulated and to correlate the various functional properties to structural features, it is necessary to determine the primary structures of these subunits.There are c...

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“…Tel. : 513-559-7223; Fax: 513-559-7868. detected in mouse skeletal muscle, brain, and cardiac tissues but not in liver, consistent with tissue-specific expression of the muscle enzyme (10). The tissue-specific expression of PhK may be related to the presence of distinct PhK isozymes.…”

mentioning

confidence: 62%

The Testis Isoform of the Phosphorylase Kinase Catalytic Subunit (PhK-γT) Plays a Critical Role in Regulation of Glycogen Mobilization in Developing Lung

Liu

Rannels

Falconieri

et al. 1996

Journal of Biological Chemistry

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In order to identify the form of phosphorylase kinase catalytic subunit expressed in developing lung, degenerate polymerase chain reaction primers were designed based on conserved domains of the two known catalytic subunits, expressed primarily in muscle and testis. Amplification of cDNA from day 19 fetal rat lung followed by cloning and sequence analyses indicated that only the testis isoform of phosphorylase kinase (PhK-␥T) was detectable in fetal lung. In situ hybridization analyses indicated that expression of PhK-␥T RNA in developing lung tissue was widespread and not restricted to Type II epithelial cells; PhK-␥T protein expression was temporally and spatially correlated with expression of PhK-␥T RNA. PhK-␥T RNA and protein expression was also characterized in the PhK-deficient glycogen storage disease (gsd) rat. PhK-␥T RNA levels were similar in Type II cells isolated from wild type and gsd/gsd fetuses; in contrast, PhK-␥T protein was virtually undetectable in gsd/ gsd Type II cells and enzyme activity was very low. These results suggest that PhK-␥T plays a critical role in mobilization of glycogen during fetal lung development and that failure to catabolize glycogen in the gsd/gsd rat is related to an untranslatable PhK-␥T RNA or unstable protein.

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Isolation of cDNA clones for the catalytic gamma subunit of mouse muscle phosphorylase kinase: expression of mRNA in normal and mutant Phk mice.

Abstract: We have isolated and characterized cDNA clones for the y subunit of mouse muscle phosphorylase kinase

Cited by 50 publications

References 35 publications

Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure

Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure

cDNA cloning and complete primary structure of skeletal muscle phosphorylase kinase (alpha subunit).

The Testis Isoform of the Phosphorylase Kinase Catalytic Subunit (PhK-γT) Plays a Critical Role in Regulation of Glycogen Mobilization in Developing Lung

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