A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation.

By S. Frame, P. Cohen, R. Biondi. Molecules and Cells, 2001

706 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/653681f6dd42dd4f3dd5148a46bc37bbc8605579

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Citations in the corpus

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease (2015, positive): “Two GSK-3 isoforms exist, GSK-3α and GSK-3β, both of which are inhibited by growth factors via Akt phosphorylation of their N-terminal Ser-21 and Ser-9 residues, respectively; inhibition of GSK-3 upon phosphorylation occurs because the modified N-terminal region acts as a pseudo-substrate and compet”
The β-catenin destruction complex. (2013, background): “GSK-3 phosphorylates residues in the sequence S/T-X-X-X-pS/pT, in which the bold residue represents the phosphorylation site, and X is any amino acid (Fiol et al. 1987; Frame et al. 2001).”
Diet‐induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease (2004, background): “AKT/PKB kinase activity as reflected by phosphorylation of the pS(473) residue primarily results in the inhibition of GSK-3α and GSK-3β activities via N-terminal pS(21) and pS(9) phosphorylation, respectively (33).”
Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. (2006, background): “Phosphorylation by AKT at the GSK-3 N terminus generates a ‘‘pseudosubstrate,’’ self-inhibiting GSK-3 by occupying its active center (Frame et al., 2001).”
The protein kinase Akt induces epithelial mesenchymal transition and promotes enhanced motility and invasiveness of squamous cell carcinoma lines. (2003, background): “The apparent discrepancy can be resolved by recent crystallographic and biochemical studies elucidating the mechanisms of GSK3 regulation (52, 53): Wnt and insulin/AKT signaling pathways affect two distinct pools of GSK3 that in turn target different substrates, thereby giving selective responses an”
Protein kinases — the major drug targets of the twenty-first century? (2002, background): “Unlike ATP competitive inhibitors, such compounds might have the potential to prevent a protein kinase from phosphorylating some substrates but not other”
Mechanisms of specificity in protein phosphorylation (2007, background): “The primed phosphorylation motif binds to a docking groove on GSK3 that is adjacent to the catalytic cleft of GSK3 (Ref”
Axin-mediated CKI phosphorylation of beta-catenin at Ser 45: a molecular switch for the Wnt pathway. (2002, methodology): “This indicates, that contrary to prevailing models (Ali et al. 2001; Cohen and Frame 2001; Dajani et al. 2001; Frame et al. 2001; Harwood, 2001), association with axin does not substitute for the +4p priming of GSK3.”
Role of tau protein in both physiological and pathological conditions. (2004, background): “Two types of GSK3 phosphorylation have been proposed: primed (following prior phosphorylation of the substrate by another kinase) or unprimed phosphorylation (75).”
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling (2005, background): “where the N-terminus of GSK3 was shown to be converted to an autoinhibitory pseudo-substrate via the phosphorylation of Ser9 (Dajani et al., 2001; Frame et al., 2001).”