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Gene Review:

FRAT2 - frequently rearranged in advanced T-cell...

Homo sapiens

Synonyms: FRAT-2, Frequently rearranged in advanced T-cell lymphomas 2, GSK-3-binding protein FRAT2

Saitoh, T. et al., Stoothoff, W.H. et al., Freemantle, S.J. et al., Saitoh, T. et al., Saitoh, T. et al.

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Disease relevance of FRAT2

FRAT1 and FRAT2 mRNAs are up-regulated together in a gastric cancer cell line TMK1, and also in 2 out of 10 cases of primary gastric cancer [1].
1. The FRAT2 mRNA of 2.4-kb in size was relatively highly expressed in MKN45 (gastric cancer), HeLa S3 (cervical cancer), and K-562 (chronic myelogenous leukemia) [2].

High impact information on FRAT2

Further, in vitro assays using recombinant proteins directly demonstrated that FRAT-2 enhances GSK3 beta-mediated phosphorylation of a primed substrate to a greater extent than an unprimed substrate [3].
Characterization and tissue-specific expression of human GSK-3-binding proteins FRAT1 and FRAT2 [4].
We have isolated the entire coding sequence of human FRAT2 (frequently rearranged in advanced T-cell lymphomas-2) [4].
The FRAT2 gene was mapped to human chromosome 10q24 [2].
Thus, up-regulation of FRAT2 in human cancer might be implicated in carcinogenesis through activation of the WNT signaling pathway [2].

Biological context of FRAT2

Both hFRAT1 and hFRAT2 are intronless genes localized to the same portion of chromosome 10q24.1 and separated by only 10.7 kb [4].
Here, we have cloned FRAT2 cDNAs, spanning the complete coding sequence, from a human fetal lung cDNA library [2].
Blast search revealed that FRAT1 and FRAT2 genes, consisting of a single exon, were located together on human genome draft sequences AC006098.1 and AL355490.7, corresponding to the human chromosome 10q24.1 region [5].
However, the effects of FRAT-2 on GSK3 beta activity and tau phosphorylation have not been examined [3].

Associations of FRAT2 with chemical compounds

FRAT2 and FRAT1 were more homologous in the acidic domain (96% identity), the proline-rich domain (92% identity), and the GSK-3beta binding domain (100% identity) [2].

Enzymatic interactions of FRAT2

In addition, FRAT-2 is phosphorylated by GSK3 beta [3].

Analytical, diagnostic and therapeutic context of FRAT2

Molecular cloning and characterization of FRAT2, encoding a positive regulator of the WNT signaling pathway [2].
Co-immunoprecipitation studies revealed that association of FRAT-2 with GSK3 beta resulted in a significant increase in phosphorylation of a primed substrate but did not alter phosphorylation of an unprimed substrate [3].

References

Molecular cloning and expression of proto-oncogene FRAT1 in human cancer. Saitoh, T., Mine, T., Katoh, M. Int. J. Oncol. (2002) [Pubmed]
Molecular cloning and characterization of FRAT2, encoding a positive regulator of the WNT signaling pathway. Saitoh, T., Moriwaki, J., Koike, J., Takagi, A., Miwa, T., Shiokawa, K., Katoh, M. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
FRAT-2 preferentially increases glycogen synthase kinase 3 beta-mediated phosphorylation of primed sites, which results in enhanced tau phosphorylation. Stoothoff, W.H., Cho, J.H., McDonald, R.P., Johnson, G.V. J. Biol. Chem. (2005) [Pubmed]
Characterization and tissue-specific expression of human GSK-3-binding proteins FRAT1 and FRAT2. Freemantle, S.J., Portland, H.B., Ewings, K., Dmitrovsky, F., DiPetrillo, K., Spinella, M.J., Dmitrovsky, E. Gene (2002) [Pubmed]
FRAT1 and FRAT2, clustered in human chromosome 10q24.1 region, are up-regulated in gastric cancer. Saitoh, T., Katoh, M. Int. J. Oncol. (2001) [Pubmed]

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FRAT2	Bos taurus
FRAT2	Macaca mulatta
Frat2	Mus musculus
FRAT2	Pan troglodytes
Frat2	Rattus norvegicus

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