Glycogen Synthase Kinase-3 (GSK-3) is Implicated in the Regulation of Initiation Factor 2B Activity in Insulin-like Growth Factor-1-stimulated Neuronal Cells

2000 ◽  
Vol 28 (5) ◽  
pp. A340-A340
Author(s):  
Celia Quevedo ◽  
Alberto Alcazar ◽  
Cristina Martin-de-la-Vega ◽  
Matilde Salinas
Keyword(s):  
Growth Factor ◽  
Glycogen Synthase ◽  
Neuronal Cells ◽  
Glycogen Synthase Kinase ◽  
Initiation Factor ◽  
Glycogen Synthase Kinase 3 ◽  
Insulin Like Growth Factor

scholarly journals Glycogen synthase kinase-3 regulates endoplasmic reticulum (ER) stress-induced CHOP expression in neuronal cells

2011 ◽  
Vol 317 (11) ◽  
pp. 1621-1628 ◽  
Author(s):  
Gordon P. Meares ◽  
Marjelo A. Mines ◽  
Eléonore Beurel ◽  
Tae-Yeon Eom ◽  
Ling Song ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Er Stress ◽  
Glycogen Synthase ◽  
Neuronal Cells ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Chop Expression

scholarly journals The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bɛ at Ser539 and the microtubule-associated protein tau at Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming kinase

2001 ◽  
Vol 355 (3) ◽  
pp. 609-615 ◽  
Author(s):  
Yvonne L. WOODS ◽  
Philip COHEN ◽  
Walter BECKER ◽  
Ross JAKES ◽  
Michel GOEDERT ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Kinases ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Initiation Factor ◽  
Glycogen Synthase Kinase 3 ◽  
General Role ◽  
Protein Tau ◽  
Microtubule Associated Protein Tau ◽  
Protein Synthesis Initiation

The substrate specificity of glycogen synthase kinase 3 (GSK3) is unusual in that efficient phosphorylation only occurs if another phosphoserine or phosphothreonine residue is already present four residues C-terminal to the site of GSK3 phosphorylation. One such substrate is the ε-subunit of rat eukaryotic protein-synthesis initiation factor 2B (eIF2Bε), which is inhibited by the GSK3-catalysed phosphorylation of Ser535. There is evidence that GSK3 is only able to phosphorylate eIF2Bε at Ser535 if Ser539 is already phosphorylated by another protein kinase. However, no protein kinases capable of phosphorylating Ser539 have so far been identified. Here we show that Ser539 of eIF2Bε, which is followed by proline, is phosphorylated specifically by two isoforms of dual-specificity tyrosine phosphorylated and regulated kinase (DYRK2 and DYRK1A), but only weakly or not at all by other ‘proline-directed’ protein kinases tested. We also establish that phosphorylation of Ser539 permits GSK3 to phosphorylate Ser535in vitro and that eIF2Bε is highly phosphorylated at Ser539in vivo. The DYRK isoforms also phosphorylate human microtubule-associated protein tau at Thr212in vitro, a residue that is phosphorylated in foetal tau and hyperphosphorylated in filamentous tau from Alzheimer's-disease brain. Phosphorylation of Thr212 primes tau for phosphorylation by GSK3 at Ser208in vitro, suggesting a more general role for DYRK isoforms in priming phosphorylation of GSK3 substrates.

scholarly journals Glycogen Synthase Kinase-3β is Involved in the Process of Myocardial Hypertrophy Stimulated by Insulin-Like Growth Factor-1

2004 ◽  
Vol 68 (3) ◽  
pp. 247-253 ◽  
Author(s):  
Satomi-Kobayashi Seimi ◽  
Kawashima Seinosuke ◽  
Sakoda Tsuyoshi ◽  
Ueyama Tomomi ◽  
Hirase Tetsuaki ◽  
...  
Keyword(s):  
Growth Factor ◽  
Myocardial Hypertrophy ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Insulin Like Growth Factor ◽  
Glycogen Synthase Kinase 3Β

scholarly journals The Fibroblast Growth Factor 14·Voltage-gated Sodium Channel Complex Is a New Target of Glycogen Synthase Kinase 3 (GSK3)

2013 ◽  
Vol 288 (27) ◽  
pp. 19370-19385 ◽  
Author(s):  
Alexander S. Shavkunov ◽  
Norelle C. Wildburger ◽  
Miroslav N. Nenov ◽  
Thomas F. James ◽  
Tetyana P. Buzhdygan ◽  
...  
Keyword(s):  
Growth Factor ◽  
Sodium Channel ◽  
Fibroblast Growth Factor ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Fibroblast Growth ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated
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