Galectin-4 is involved in p27-mediated activation of the myelin basic protein promoter

Qiou Wei, Tamar Eviatar-Ribak, W. Keith Miskimins, Robin Miskimins

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1214-1223
Number of pages10
JournalJournal of Neurochemistry
Issue number5
StatePublished - Jun 2007
Externally publishedYes


  • Galectin
  • Myelin basic protein
  • Sp1
  • Transcriptional control
  • p27

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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