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

Amos Charles, Xiaoren Tang, Erika Crouch, Jerome S. Brody, Zhi Xiong Jim Xiao

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


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/EBPβ) binding motif in the human SP-D promoter, and this sequence specifically bound to C/EBPα, C/EBPβ, and C/EBPδ. 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.

Original languageEnglish
Pages (from-to)414-425
Number of pages12
JournalJournal of cellular biochemistry
Issue number3
StatePublished - 2001


  • C/EBP
  • Differentiation
  • Retinoblastoma protein
  • Surfactant protein D
  • Transcription


Dive into the research topics of 'Retinoblastoma protein complexes with C/EBP proteins and activates C/EBP-mediated transcription'. Together they form a unique fingerprint.

Cite this