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A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of Axin and β-catenin

FEBS letters, 1999-09, Vol.458 (2), p.247-251 [Peer Reviewed Journal]

1999 Federation of European Biochemical Societies ;FEBS Letters 458 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies ;ISSN: 0014-5793 ;EISSN: 1873-3468 ;DOI: 10.1016/S0014-5793(99)01161-8 ;PMID: 10481074

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Title:
A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of Axin and β-catenin
Author: Thomas, Gareth M. ; Frame, Sheelagh ; Goedert, Michel ; Nathke, Inke ; Polakis, Paul ; Cohen, Philip
Subjects: Amino Acid Sequence ; Animals ; Axin ; Axin Protein ; beta Catenin ; Binding, Competitive ; Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Calcium-Calmodulin-Dependent Protein Kinases - physiology ; Carrier Proteins - metabolism ; Catalysis ; Cell Line ; Cytoskeletal Proteins - antagonists & inhibitors ; Cytoskeletal Proteins - metabolism ; Embryonic and Fetal Development - physiology ; Enzyme Inhibitors - metabolism ; FRAT1 ; Glycogen Synthase Kinase 3 ; Glycogen Synthase Kinases ; Humans ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; Neoplasm Proteins ; Peptide Fragments - metabolism ; Phosphorylation ; Proteins - antagonists & inhibitors ; Proteins - metabolism ; Proto-Oncogene Proteins - metabolism ; Repressor Proteins ; Sequence Homology, Amino Acid ; Signal Transduction - physiology ; Trans-Activators ; Xenopus Proteins ; β-Catenin
Is Part Of: FEBS letters, 1999-09, Vol.458 (2), p.247-251
Description: The Axin-dependent phosphorylation of β-catenin catalysed by glycogen synthase kinase-3 (GSK3) is inhibited during embryogenesis. This protects β-catenin against ubiquitin-dependent proteolysis, leading to its accumulation in the nucleus, where it controls the expression of genes important for development. Frequently rearranged in advanced T-cell lymphomas 1 (FRAT1) is a mammalian homologue of a GSK3-binding protein (GBP), which appears to play a key role in the correct establishment of the dorsal-ventral axis in Xenopus laevis. Here, we demonstrate that FRATtide (a peptide corresponding to residues 188–226 of FRAT1) binds to GSK3 and prevents GSK3 from interacting with Axin. FRATtide also blocks the GSK3-catalysed phosphorylation of Axin and β-catenin, suggesting a potential mechanism by which GBP could trigger axis formation. In contrast, FRATtide does not suppress GSK3 activity towards other substrates, such as glycogen synthase and eIF2B, whose phosphorylation is independent of Axin but dependent on a ‘priming’ phosphorylation. This may explain how the essential cellular functions of GSK3 can continue, despite the suppression of β-catenin phosphorylation.
Publisher: England: Elsevier B.V
Language: English
Identifier: ISSN: 0014-5793
EISSN: 1873-3468
DOI: 10.1016/S0014-5793(99)01161-8
PMID: 10481074
Source: GFMER Free Medical Journals
MEDLINE
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A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of Axin and β-catenin

1999 Federation of European Biochemical Societies ;FEBS Letters 458 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies ;ISSN: 0014-5793 ;EISSN: 1873-3468 ;DOI: 10.1016/S0014-5793(99)01161-8 ;PMID: 10481074

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