scholarly journals AMP-activated protein kinase (AMPK) activating agents cause dephosphorylation of Akt and glycogen synthase kinase-3

2006 ◽  
Vol 71 (11) ◽  
pp. 1637-1647 ◽  
Author(s):  
Taj D. King ◽  
Ling Song ◽  
Richard S. Jope
Keyword(s):  
Protein Kinase ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Amp Activated Protein Kinase

scholarly journals Resveratrol Improves Cardiac Functions of the Diabetic Cardiomyopathy Rats Via Modulation of AMP-Activated Protein Kinase and the Phosphorylated Glycogen Synthase Kinase-3(3

2019 ◽  
Vol 87 (September) ◽  
pp. 2827-2837
Author(s):  
HEND ASHOUR, M.D.; ASMAA M. SHAMSELDEEN, M.D. ◽  
HEBA S. SHOUKRY, M.D.; LAILA A. RASHED, M.D. ◽  
MOHAMED M. EL-SEBAIE, M.D.; MOHAMED H. ELSAYED, M.Sc. ◽  
SHEREEN ABDELFATTAH, M.D.; SAFINAZ SALAH-ELDIN, M.D. ◽  
HANIA I. AMMAR, M.D.
Keyword(s):  
Protein Kinase ◽  
Diabetic Cardiomyopathy ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Cardiac Functions ◽  
Amp Activated Protein Kinase

scholarly journals Inhibition of Insulin-Stimulated Glycogen Synthesis by 5-Aminoimidasole-4-Carboxamide-1-β-d-Ribofuranoside-Induced Adenosine 5′-Monophosphate-Activated Protein Kinase Activation: Interactions with Akt, Glycogen Synthase Kinase 3-3α/β, and Glycogen Synthase in Isolated Rat Soleus Muscle

Endocrinology ◽  
2006 ◽  
Vol 147 (11) ◽  
pp. 5170-5177 ◽  
Author(s):  
S. Fediuc ◽  
M. P. Gaidhu ◽  
R. B. Ceddia
Keyword(s):  
Protein Kinase ◽  
Glycogen Content ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Lactate Production ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Kinase Activation ◽  
Protein Kinase Activation ◽  
Amp Activated Protein Kinase

The aim of this study was to investigate the effects of 5-aminoimidasole-4-carboxamide-1-β-d-ribofuranoside (AICAR)-induced AMP-activated protein kinase activation on glycogen metabolism in soleus (slow twitch, oxidative) and epitrochlearis (fast twitch, glycolytic) skeletal muscles. Isolated soleus and epitrochlearis muscles were incubated in the absence or presence of insulin (100 nm), AICAR (2 mm), and AICAR plus insulin. In soleus muscles exposed to insulin, glycogen synthesis and glycogen content increased 6.4- and 1.3-fold, respectively. AICAR treatment significantly suppressed (∼60%) insulin-stimulated glycogen synthesis and completely prevented the increase in glycogen content induced by insulin. AICAR did not affect either basal or insulin-stimulated glucose uptake but significantly increased insulin-stimulated (∼20%) lactate production in soleus muscles. Interestingly, basal glucose uptake was significantly increased (∼1.4-fold) in the epitrochlearis muscle, even though neither basal nor insulin-stimulated rates of glycogen synthesis, glycogen content, and lactate production were affected by AICAR. We also report the novel evidence that AICAR markedly reduced insulin-induced Akt-Thr308 phosphorylation after 15 and 30 min exposure to insulin, which coincided with a marked reduction in glycogen synthase kinase 3 (GSK)-3α/β phosphorylation. Importantly, phosphorylation of glycogen synthase was increased by AICAR treatment 45 min after insulin stimulation. Our results indicate that AICAR-induced AMP-activated protein kinase activation caused a time-dependent reduction in Akt308 phosphorylation, activation of glycogen synthase kinase-3α/β, and the inactivation of glycogen synthase, which are compatible with the acute reduction in insulin-stimulated glycogen synthesis in oxidative but not glycolytic skeletal muscles.

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 Multiple mechanisms for the phosphorylation of C-terminal regulatory sites in rabbit muscle glycogen synthase expressed in COS cells

1996 ◽  
Vol 313 (1) ◽  
pp. 45-50 ◽  
Author(s):  
Alexander V. SKURAT ◽  
Peter J. ROACH
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Rabbit Muscle ◽  
Cos Cells ◽  
Additional Mutation ◽  
Regulatory Sites

Glycogen synthase can be inactivated by sequential phosphorylation at the C-terminal residues Ser652 (site 4), Ser648 (site 3c), Ser644 (site 3b) and Ser640 (site 3a) catalysed by glycogen synthase kinase-3. In vitro, glycogen synthase kinase-3 action requires that glycogen synthase has first been phosphorylated at Ser656 (site 5) by casein kinase II. Recently we demonstrated that inactivation is linked only to phosphorylation at site 3a and site 3b, and that, in COS cells, modification of these sites can occur by alternative mechanisms independent of any C-terminal phosphorylations [Skurat and Roach (1995) J. Biol. Chem. 270, 12491-12497]. To address these mechanisms multiple Ser → Ala mutations were introduced in glycogen synthase such that only site 3a or site 3b remained intact. Additional mutation of Arg637 → Gln eliminated phosphorylation of site 3a, indicating that Arg637 may be important for recognition of site 3a by its corresponding protein kinase(s). Similarly, additional mutation of Pro645 → Ala eliminated phosphorylation of site 3b, indicating a possible involvement of ‘proline-directed’ protein kinase(s). Mutation of Arg637 alone did not activate glycogen synthase as expected from the loss of phosphorylation at site 3a. Rather, mutation of both Arg637 and the Ser → Ala substitution at site 3b was required for substantial activation. The results suggest that sites 3a and 3b can be phosphorylated independently of one another by distinct protein kinases. However, phosphorylation of site 3b can potentiate phosphorylation of site 3a, by an enzyme such as glycogen synthase kinase-3.

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