Mouse disabled 2 interacting protein 2 functions as a transcriptional repressor through direct binding onto its own promoter

Biochem Biophys Res Commun. 2005 Nov 11;337(1):75-81. doi: 10.1016/j.bbrc.2005.08.262.

Abstract

The mDaIP2 protein is a mouse orthologue of human Nostrin (a regulator of eNos). The absence of eNos activity in RA-treated F9 cell implies that the protein plays somehow different role from Nostrin. In this experiment, this protein has been shown to repress the expression of its own gene, via a feedback mechanism which involves binding to the promoter region. Data from cotransfection, DNAP, mDaIP2-silenced F9 cell, and EMSA analyses clearly support the repression activity and direct binding of the protein to the promoter region. The protein contains N-terminal FCH domain and C-terminal SH3 domain. The SH3 domain is known to interact with the proline-rich domain of mDab2, while even no function has been reported about the FCH domain. Here, we report a novel function of mDaIP2 as a transcriptional repressor and suggest the possible association of the FCH domain with transcriptional regulation.

MeSH terms

  • 5' Flanking Region
  • Adaptor Proteins, Signal Transducing
  • Animals
  • Binding Sites
  • Cell Differentiation
  • Cell Line, Tumor
  • DNA-Binding Proteins
  • Electrophoretic Mobility Shift Assay
  • Gene Expression Regulation*
  • Mice
  • Nitric Oxide Synthase / antagonists & inhibitors
  • Nitric Oxide Synthase / genetics*
  • Nitric Oxide Synthase / metabolism*
  • Promoter Regions, Genetic*
  • RNA Interference
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*
  • Transcription, Genetic

Substances

  • Adaptor Proteins, Signal Transducing
  • DNA-Binding Proteins
  • Nostrin protein, mouse
  • Repressor Proteins
  • Nitric Oxide Synthase