The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation (Q27636657)

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C Lewis

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A R Guy

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A Bridges

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R Tanner

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G Pettman

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C Mannix

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A A Culbert

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M J Brown

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D G Smith

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A D Reith

Glycogen Synthase Kinase-3 from Rabbit Skeletal Muscle

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language of work or name

English

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publication date

December 2001

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1143-52

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Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin

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

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Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta -catenin and promotes GSK-3beta -dependent phosphorylation of beta -catenin

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Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3β

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Interaction of axin and Dvl-2 proteins regulates Dvl-2-stimulated TCF-dependent transcription.

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Bridging of β-catenin and glycogen synthase kinase-3β by Axin and inhibition of β-catenin-mediated transcription

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7 January 2021

Activation of a novel proto-oncogene, Frat1, contributes to progression of mouse T-cell lymphomas

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GBP, an Inhibitor of GSK-3, Is Implicated in Xenopus Development and Oncogenesis

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Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1.

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Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain

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Wnt-induced dephosphorylation of axin releases beta-catenin from the axin complex

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A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and beta-catenin

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Regulation of glycogen synthase kinase 3beta and downstream Wnt signaling by axin

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Structure of GSK3beta reveals a primed phosphorylation mechanism

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Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition

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Active and inactive protein kinases: structural basis for regulation

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Selective small molecule inhibitors of glycogen synthase kinase-3 modulate glycogen metabolism and gene transcription

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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

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The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases

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Suppression of glycogen synthase kinase activity is not sufficient for leukemia enhancer factor-1 activation

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GSK-3 inhibition by adenoviral FRAT1 overexpression is neuroprotective and induces Tau dephosphorylation and beta-catenin stabilisation without elevation of glycogen synthase activity

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The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification

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Further evidence that the inhibition of glycogen synthase kinase‐3β by IGF‐1 is mediated by PDK1/PKB‐induced phosphorylation of Ser‐9 and not by dephosphorylation of Tyr‐216

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Tyrosine dephosphorylation of glycogen synthase kinase-3 is involved in its extracellular signal-dependent inactivation

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Glycogen synthase kinase-3 beta activity is critical for neuronal death caused by inhibiting phosphatidylinositol 3-kinase or Akt but not for death caused by nerve growth factor withdrawal.

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Expression, purification, and functional analysis of the human serine protease HtrA2

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Identifiers

DOI

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Fatcat ID

release_m35mjj6bjnf2fnusz2zdgssjeq

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/m35mjj6bjnf2fnusz2zdgssjeq

24 November 2022