| First Author | Wei Q | Year | 2007 |
| Journal | J Neurochem | Volume | 101 |
| Issue | 5 | Pages | 1214-23 |
| PubMed ID | 17403142 | Mgi Jnum | J:122580 |
| Mgi Id | MGI:3714699 | Doi | 10.1111/j.1471-4159.2007.04488.x |
| Citation | Wei Q, et al. (2007) Galectin-4 is involved in p27-mediated activation of the myelin basic protein promoter. J Neurochem 101(5):1214-23 |
| abstractText | Our previous studies have found that expression of p27 in oligodendrocytes enhances myelin basic protein (MBP) gene expression through a mechanism that involves the transcription factor Sp1. In this study we show that this activation only requires the N-terminal 45 amino acids of p27 containing a functional cyclin-binding motif. In an effort to identify other cofactors that are involved in the p27-mediated activation of MBP gene expression, a yeast two-hybrid assay was performed using an N-terminal truncated p27 and a mouse embryo cDNA library. Galectin-4 was found to interact with p27 in the yeast two-hybrid assay. This novel interaction was also confirmed using a glutathione-S-transferase interaction assay and immunoprecipitation assays. Expression of galectin-4 in primary oligodendrocytes was confirmed by western blot. Additionally, the MBP promoter could be activated by expression of galectin-4 in CG4 oligodendrocytes, similar to the effects of increased p27 levels. We also show that Sp1 and galectin-4 interact in cells, while a complex of all three proteins could not be found. We conclude that galectin-4 is involved in the p27-mediated activation of the MBP gene, possibly through modulation of the glycosylation status of the transcription factor Sp1. |
