Isoform differences in substrate recognition by glycogen synthase kinases 3.alpha. and 3.beta. in the phosphorylation of phosphatase inhibitor 2

Biochemistry ◽  
1994 ◽  
Vol 33 (1) ◽  
pp. 143-147 ◽  
Author(s):  
Q. May Wang ◽  
In Kyung Park ◽  
Carol J. Fiol ◽  
Peter J. Roach ◽  
Anna A. DePaoli-Roach
Keyword(s):  
Glycogen Synthase ◽  
Substrate Recognition ◽  
Phosphatase Inhibitor ◽  
Glycogen Synthase Kinases

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.

scholarly journals Glycogen synthase kinases-3β controls differentiation of malignant glioma cells

2009 ◽  
Vol 127 (6) ◽  
pp. 1271-1282 ◽  
Author(s):  
Yan Li ◽  
Huimin Lu ◽  
Yijun Huang ◽  
Ru Xiao ◽  
Xiaofeng Cai ◽  
...  
Keyword(s):  
Malignant Glioma ◽  
Glycogen Synthase ◽  
Glioma Cells ◽  
Malignant Glioma Cells ◽  
Glycogen Synthase Kinases

scholarly journals Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Jennifer L Stamos ◽  
Matthew Ling-Hon Chu ◽  
Michael D Enos ◽  
Niket Shah ◽  
William I Weis
Keyword(s):  
Signaling Pathways ◽  
Glycogen Synthase ◽  
Substrate Recognition ◽  
Glycogen Synthase Kinase 3 ◽  
Structural Basis ◽  
Amino Terminus ◽  
Target Sequence ◽  
Inhibitory Peptide ◽  
Conserved Sequence ◽  
N Terminus

Glycogen synthase kinase-3 (GSK-3) is a key regulator of many cellular signaling pathways. Unlike most kinases, GSK-3 is controlled by inhibition rather than by specific activation. In the insulin and several other signaling pathways, phosphorylation of a serine present in a conserved sequence near the amino terminus of GSK-3 generates an auto-inhibitory peptide. In contrast, Wnt/β-catenin signal transduction requires phosphorylation of Ser/Pro rich sequences present in the Wnt co-receptors LRP5/6, and these motifs inhibit GSK-3 activity. We present crystal structures of GSK-3 bound to its phosphorylated N-terminus and to two of the phosphorylated LRP6 motifs. A conserved loop unique to GSK-3 undergoes a dramatic conformational change that clamps the bound pseudo-substrate peptides, and reveals the mechanism of primed substrate recognition. The structures rationalize target sequence preferences and suggest avenues for the design of inhibitors selective for a subset of pathways regulated by GSK-3.

scholarly journals Interplay Between CMGC Kinases Targeting SR Proteins and Viral Replication: Splicing and Beyond

2021 ◽  
Vol 12 ◽  
Author(s):  
Florentin Pastor ◽  
Lulzim Shkreta ◽  
Benoit Chabot ◽  
David Durantel ◽  
Anna Salvetti
Keyword(s):  
Viral Replication ◽  
Common Property ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Glycogen Synthase ◽  
Regulation Of Gene Expression ◽  
Sr Proteins ◽  
Post Translational Modification ◽  
Mitogen Activated Protein ◽  
Glycogen Synthase Kinases

Protein phosphorylation constitutes a major post-translational modification that critically regulates the half-life, intra-cellular distribution, and activity of proteins. Among the large number of kinases that compose the human kinome tree, those targeting RNA-binding proteins, in particular serine/arginine-rich (SR) proteins, play a major role in the regulation of gene expression by controlling constitutive and alternative splicing. In humans, these kinases belong to the CMGC [Cyclin-dependent kinases (CDKs), Mitogen-activated protein kinases (MAPKs), Glycogen synthase kinases (GSKs), and Cdc2-like kinases (CLKs)] group and several studies indicate that they also control viral replication via direct or indirect mechanisms. The aim of this review is to describe known and emerging activities of CMGC kinases that share the common property to phosphorylate SR proteins, as well as their interplay with different families of viruses, in order to advance toward a comprehensive knowledge of their pro- or anti-viral phenotype and better assess possible translational opportunities.

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