Characterization of GSK-M, a glycogen synthase kinase from rat skeletal muscle

1987 ◽  
Vol 258 (2) ◽  
pp. 470-481 ◽  
Author(s):  
Mohammed G. Hegazy ◽  
Thomas J. Thysseril ◽  
Keith K. Schlender ◽  
Erwin M. Reimann
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Rat Skeletal Muscle

Isolation and characterization of cyclic AMP-independent glycogen synthase kinase from rat skeletal muscle

1980 ◽  
Vol 615 (2) ◽  
pp. 324-340 ◽  
Author(s):  
Keith K. Schlender ◽  
Stephen J. Beebee ◽  
James C. Willey ◽  
Stephen A. Lutz ◽  
Erwin M. Reimann
Keyword(s):  
Skeletal Muscle ◽  
Cyclic Amp ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Rat Skeletal Muscle ◽  
Isolation And Characterization

scholarly journals Characterization of insulin-stimulated seryl/threonyl protein kinases in rat skeletal muscle

1993 ◽  
Vol 268 (18) ◽  
pp. 13203-13213
Author(s):  
Y.J. Hei ◽  
J.H. McNeill ◽  
J.S. Sanghera ◽  
J. Diamond ◽  
M. Bryer-Ash ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinases ◽  
Rat Skeletal Muscle

Characterization of β-adrenoceptors on rat skeletal muscle cells grown in vitro

1990 ◽  
Vol 40 (5) ◽  
pp. 1043-1048 ◽  
Author(s):  
Marie-Helene Disatnik ◽  
Sanford R. Sampson ◽  
Asher Shainberg
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Rat Skeletal Muscle

Analysis of RIM11, a yeast protein kinase that phosphorylates the meiotic activator IME1

1994 ◽  
Vol 14 (12) ◽  
pp. 7909-7919 ◽  
Author(s):  
K S Bowdish ◽  
H E Yuan ◽  
A P Mitchell
Keyword(s):  
Protein Kinase ◽  
Immune Complexes ◽  
Functional Relationship ◽  
Biological Function ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Yeast Protein ◽  
Yeast Genes

Many yeast genes that are essential for meiosis are expressed only in meiotic cells. Known regulators of early meiotic genes include IME1, which is required for their expression, and SIN3 and UME6, which prevent their expression in nonmeiotic cells. We report here the molecular characterization of the RIM11 gene, which we find is required for expression of several early meiotic genes. A close functional relationship between RIM11 and IME1 is supported by two observations. First, sin3 and ume6 mutations are epistatic to rim11 mutations; prior studies have demonstrated their epistasis to ime1 mutations. Second, overexpression of RIM11 can suppress an ime1 missense mutation (ime1-L321F) but not an ime1 deletion. Sequence analysis indicates that RIM11 specifies a protein kinase related to rat glycogen synthase kinase 3 and the Drosophila shaggy/zw3 gene product. Three partially defective rim11 mutations alter residues involved in ATP binding or catalysis, and a completely defective rim11 mutation alters a tyrosine residue that corresponds to the site of an essential phosphorylation for glycogen synthase kinase 3. Immune complexes containing a hemagglutinin (HA) epitope-tagged RIM11 derivative, HA-RIM11, phosphorylate two proteins, p58 and p60, whose biological function is undetermined. In addition, HA-RIM11 immune complexes phosphorylate a functional IME1 derivative but not the corresponding ime1-L321F derivative. We propose that RIM11 stimulates meiotic gene expression through phosphorylation of IME1.

scholarly journals Control of rat skeletal-muscle phosphorylase phosphatase activity by adrenaline

1978 ◽  
Vol 176 (1) ◽  
pp. 347-350 ◽  
Author(s):  
S H Tao ◽  
F L Huang ◽  
A Lynch ◽  
W H Glinsmann
Keyword(s):  
Skeletal Muscle ◽  
Cyclic Amp ◽  
Phosphatase Activity ◽  
Glycogen Synthase ◽  
Rat Skeletal Muscle ◽  
Inhibitor Activity ◽  
Phosphatase Inhibitor ◽  
Heat Stable ◽  
Muscle Phosphorylase ◽  
Isolated Rat

Administration of adrenaline to an isolated rat hindlimb preparation rapidly decreased muscle phosphorylase phosphatase (EC 3.1.3.17) activity and increased heat-stable and trypsin-labile phosphatase inhibitor activity. This was associated with increased tissue cyclic AMP concentrations, phosphorylase (EC 2.4.1.1) activation and glycogen synthase (EC 2.4.1.11) inactivation.

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