The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
A GSK3‐binding peptide from FRAT1 selectively inhibits the GSK3‐catalysed phosphorylation of Axin and β‐catenin
Open accessAbstract
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.
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Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
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Self-citationTranscriptional Cross Talk between NF-κB and p53
Webster, G. A., & Perkins, N. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3485 · Cited by 598
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Self-citationYamamoto, H., Kishida, S., Kishida, M., Ikeda, S., Takada, S., & Kikuchi, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10681 · Cited by 364
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Cited by
Polakis, P. (2000) · Genes & Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183
GSK-3: tricks of the trade for a multi-tasking kinase
Doble, B. W., & Woodgett, J. R. (2003) · Journal of Cell Science · doi:10.1242/jcs.00384 · Cited by 2,084
Control of β-Catenin Phosphorylation/Degradation by a Dual-Kinase Mechanism
Liu, C., Li, Y., Semenov, M., Han, C., Baeg, G.-H., Tan, Y., Zhang, Z., Lin, X., & He, X. (2002) · Cell · doi:10.1016/s0092-8674(02)00685-2 · Cited by 2,069
Phiel, C. J., Zhang, F., Huang, E. Y., Guenther, M. G., Lazar, M. A., & Klein, P. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101287200 · Cited by 1,758
GSK3 takes centre stage more than 20 years after its discovery
FRAME, S., & COHEN, P. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590001 · Cited by 1,433
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Metadata
- Authors
- Thomas, G. M., Frame, S., Goedert, M., Nathke, I., Polakis, P., & Cohen, P.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-09-10
- Volume
- 458
- Issue
- 2
- Pages
- 247-251
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2066497759
- Cited by
- 229
- References
- 7
- FWCI
- 6.42
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Thomas, G. M., Frame, S., Goedert, M., Nathke, I., Polakis, P., & Cohen, P. (1999). A GSK3‐binding peptide from FRAT1 selectively inhibits the GSK3‐catalysed phosphorylation of Axin and β‐catenin. FEBS Letters. https://doi.org/10.1016/s0014-5793(99)01161-8
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