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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Retinoblastoma protein complexes with C/EBP proteins and activates C/EBP-mediated transcription.

The retinoblastoma protein (RB) recruits histone deacetylase ( HDAC) to repress E2F-mediated transactivation that plays a critical role in cell cycle regulation. RB is also involved in activation of expression of a number of tissue specific- and differentiation-related genes. In this study, we examined the mechanism by which RB stimulated the expression of a differentiation-related gene, the surfactant protein D (SP-D), which plays important roles in innate host defense and the regulation of surfactant homeostasis. We demonstrated that RB specifically stimulated the activity of human SP-D gene promoter. The RB family member, p107 but not p130, also increased SP-D promoter activity. Activation by RB was mediated through a NF-IL6 (C/EBP beta) binding motif in the human SP-D promoter, and this sequence specifically bound to C/EBP alpha, C/EBP beta, and C/EBP delta. RB formed stable complexes with all three C/EBP family members. RB small pocket (amino acid residues 379-792), but not the C-pocket (amino acid residues 792-928), was necessary and sufficient for its interaction with C/EBP proteins. Furthermore, we demonstrated that the complexes containing RB and C/EBP proteins directly interacted with C-EBP binding site on DNA. These findings indicate that RB plays a positive, selective, and direct role in the C/EBP-dependent transcriptional regulation of human SP-D expression.[1]

References

  1. Retinoblastoma protein complexes with C/EBP proteins and activates C/EBP-mediated transcription. Charles, A., Tang, X., Crouch, E., Brody, J.S., Xiao, Z.X. J. Cell. Biochem. (2001) [Pubmed]
 
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