scholarly journals c-Src regulates cell cycle proteins expression through protein kinase B/glycogen synthase kinase 3 beta and extracellular signal-regulated kinases 1/2 pathways in MCF-7 cells

2013 ◽  
Vol 45 (7) ◽  
pp. 586-592 ◽  
Author(s):  
Xiang Liu ◽  
Liying Du ◽  
Renqing Feng
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Glycogen Synthase ◽  
Protein Kinase B ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Cell Cycle Proteins ◽  
Extracellular Signal ◽  
Mcf 7

scholarly journals Glycogen Synthase Kinase 3 Phosphorylates Hypoxia-Inducible Factor 1α and Mediates Its Destabilization in a VHL-Independent Manner

2007 ◽  
Vol 27 (9) ◽  
pp. 3253-3265 ◽  
Author(s):  
Daniela Flügel ◽  
Agnes Görlach ◽  
Carine Michiels ◽  
Thomas Kietzmann
Keyword(s):  
Protein Kinase ◽  
Metabolic Diseases ◽  
Glycogen Synthase ◽  
Protein Kinase B ◽  
Hypoxia Inducible Factor ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3 ◽  
Independent Manner ◽  
Von Hippel Lindau ◽  
Gsk 3Β

ABSTRACT Hypoxia-inducible transcription factor 1α (HIF-1α) is a key player in the response to hypoxia. Additionally, HIF-1α responds to growth factors and hormones which can act via protein kinase B (Akt). However, HIF-1α is not a direct substrate for this kinase. Therefore, we investigated whether the protein kinase B target glycogen synthase kinase 3 (GSK-3) may have an impact on HIF-1α. We found that the inhibition or depletion of GSK-3 induced HIF-1α whereas the overexpression of GSK-3β reduced HIF-1α. These effects were mediated via three amino acid residues in the oxygen-dependent degradation domain of HIF-1α. In addition, mutation analyses and experiments with von Hippel-Lindau (VHL)-defective cells indicated that GSK-3 mediates HIF-1α degradation in a VHL-independent manner. In line with these observations, the inhibition of the proteasome reversed the GSK-3 effects, indicating that GSK-3 may target HIF-1α to the proteasome by phosphorylation. Thus, the direct regulation of HIF-1α stability by GSK-3 may influence physiological processes or pathophysiological situations such as metabolic diseases or tumors.

Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

Nature ◽  
1995 ◽  
Vol 378 (6559) ◽  
pp. 785-789 ◽  
Author(s):  
Darren A. E. Cross ◽  
Dario R. Alessi ◽  
Philip Cohen ◽  
Mirjana Andjelkovich ◽  
Brian A. Hemmings
Keyword(s):  
Protein Kinase ◽  
Glycogen Synthase ◽  
Protein Kinase B ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3

scholarly journals Essential Role for Protein Kinase B (PKB) in Insulin-induced Glycogen Synthase Kinase 3 Inactivation

1998 ◽  
Vol 273 (21) ◽  
pp. 13150-13156 ◽  
Author(s):  
Pascale C. van Weeren ◽  
Kim M. T. de Bruyn ◽  
Alida M. M. de Vries-Smits ◽  
Johan van Lint ◽  
Boudewijn M. Th. Burgering
Keyword(s):  
Protein Kinase ◽  
Essential Role ◽  
Glycogen Synthase ◽  
Protein Kinase B ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3
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