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GSK3B — PSEN1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: GSK3B — PSEN1 (direct interaction, enzymatic study) Prager et al., J Biol Chem 2007*
• IRef Intact Interaction: PSEN1 — GSK3B (physical association, anti bait coimmunoprecipitation) Twomey et al., FEBS Lett 2006*

Text-mined interactions from Literome

Kang et al., J Neurosci 1999 (Adenomatous Polyposis Coli...) : Inducible overexpression of PS1 led to increased association of beta-catenin with glycogen synthase kinase-3beta ( GSK-3beta ), a negative regulator of beta-catenin, and accelerated the turnover of endogenous beta-catenin
Kirschenbaum et al., J Biol Chem 2001 : Glycogen synthase kinase-3beta regulates presenilin 1 C-terminal fragment levels
Pigino et al., J Neurosci 2003 (Alzheimer Disease) : We show that relative levels of GSK3beta activity were increased in cells either in the presence of mutant PS1 or in the absence of PS1 (PS1-/-)
Dewachter et al., Neurobiol Aging 2008 (Synaptic Transmission) : In contrast to the deficiency in PS1, mutant PS1 activated GSK-3beta by decreasing phosphorylation on Ser-9, which correlated with increased phosphorylation of protein tau at Ser-396-Ser-404 ( PHF1/AD2 epitope )
Uemura et al., J Biol Chem 2007 (Alzheimer Disease) : Glycogen synthase kinase 3beta mediated phosphorylation of Presenilin 1 reduces its binding to N-cadherin, thereby down regulating its cell-surface expression ... Because the cleavage of various membrane proteins by Presenilin 1/gamma-cleavage is involved in cellular signaling, glycogen synthase kinase 3beta mediated phosphorylation of Presenilin 1 should be deeply associated with signaling functions