Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain.
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Hsu HC, Lee YL, Cheng TS, Howng SL, Chang LK, Lu PJ, Hong YR
Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain.
Biochem Biophys Res Commun. 2005 Apr 15;329(3):1108-17.
- PubMed ID
- 15752768 [ View in PubMed]
- Abstract
To explore more possible roles for GSK3beta function, the yeast two-hybrid screening using GSK3beta as a bait protein was performed. In this study, we demonstrated that two variants of CABYR (281 and 379) interacted with GSK3beta in the yeast two-hybrid and GST pull down assay. Molecular characterization showed that CABYR variants formed a dimer with a proline-rich extensin-like domain, which slightly overlapped with GSK3beta-binding site. In kinase assay, we also showed that CABYR variants act as an ideal substrate for GSK3beta within the extensin-like domain and phosphorylation sites on CABYR were mapped. Interestingly, Northern blot showed that CABYR transcripts were expressed more distinctly in the fetal brain than in the adult brain, suggesting that this protein may play a role during brain development. Moreover, differential expression of CABYR variants may exhibit aberrant expression in brain tumors and cancer cell lines.