◀ Back to GSK3B
GSK3B — GYS2
Pathways - manually collected, often from reviews:
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OpenBEL Selventa BEL large corpus:
GYS2
→
GSK3B
(directlyIncreases, GYS2 Activity)
Evidence: Insulin Stimulated phosphorylation cascade This pathway involves the tyrosine phosphorylation of IRS proteins and/or Shc, which in turn interact with the adapter protein Grb2, recruiting the Son-of-sevenless (SOS) exchange protein to the plasma membrane for activation of Ras. The activation of Ras also requires stimulation of the tyrosine phosphatase SHP2, through its interaction with receptor substrates such as Gab-1 or IRS1/2. Activated ERK can translocate into the nucleus, where it catalyses ...
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KEGG Insulin signaling pathway:
GSK3B
→
GYS1/GYS2
(protein-protein, inhibition)
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WikiPathways Glycogen Metabolism:
GSK3B/GSK3A
→
GYS1/GYS2
(inhibition)
Text-mined interactions from Literome
Syed et al., Mol Cell Biochem 2000
:
These data suggest that stimulation of
glycogen synthase by insulin in HepG2 cells is
mediated through the PI-3 kinase pathway by activating PKB and PP-1G and inactivating
GSK-3beta
Jarvill-Taylor et al., J Am Coll Nutr 2001
:
In addition, MHCP treatment activated
glycogen synthase and
inhibited glycogen synthase kinase-3beta activities, known effects of insulin treatment
Pearce et al., Metabolism 2004
(Body Weight...) :
At 29 weeks of age,
GSK-3beta protein levels were 5-fold higher, and
glycogen synthase activation ( -27 % ), glycogen levels ( -58 % ) and insulin receptor substrate-1 (IRS-1) protein levels ( -67 % ) were significantly
reduced in skeletal muscle
Kim et al., Mol Cell Biol 2005
:
The increased
glycogen synthase activity occurs in spite of decreased signaling through the insulin receptor substrate 1 (IRS-1)-phosphoinositide (PI) 3-kinase-Akt pathway and
increased glycogen synthase kinase 3beta ( GSK3beta ) activity in the basal state
Ilouz et al., J Biol Chem 2006
:
Subsequently, expression of the
GSK-3beta mutants in cells resulted in decreased phosphorylation of substrates CREB, IRS-1, and beta-catenin, and
prevented their suppression of
glycogen synthase activity as compared with cells expressing the wild-type GSK-3beta
Kawakami et al., J Biochem 2008
:
It was found that ( i ) both PI and SH highly stimulated the
GSK-3beta mediated phosphorylation of MBP, but not
glycogen synthase , and two MBP peptides through their direct binding to these substrates and ( ii ) both PI and heparin, as compared with sulfatide, highly stimulated autophosphorylation of GSK-3beta