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Characterization of two non-testis-specific CABYR variants that bind to GSK3beta with a proline-rich extensin-like domain.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2005 Apr 15; Vol. 329 (3), pp. 1108-17. - Publication Year :
- 2005
-
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.
- Subjects :
- Amino Acid Sequence
Binding Sites
Calcium-Binding Proteins genetics
Cells, Cultured
Glycogen Synthase Kinase 3 genetics
Glycogen Synthase Kinase 3 beta
Glycoproteins metabolism
HeLa Cells
Humans
Male
Molecular Sequence Data
Organ Specificity
Phosphoproteins genetics
Plant Proteins metabolism
Protein Binding
Protein Isoforms genetics
Protein Isoforms metabolism
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Structure-Activity Relationship
Testis metabolism
Tissue Distribution
Brain metabolism
Brain Neoplasms metabolism
Calcium-Binding Proteins metabolism
Glycogen Synthase Kinase 3 metabolism
Phosphoproteins metabolism
Proline metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 329
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 15752768
- Full Text :
- https://doi.org/10.1016/j.bbrc.2005.02.089