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PMID:9178770

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Citation

Lavender, P, Vandel, L, Bannister, AJ and Kouzarides, T (1997) The HMG-box transcription factor HBP1 is targeted by the pocket proteins and E1A. Oncogene 14:2721-8

Abstract

A yeast two-hybrid screen has identified HBP1 as a transcription factor capable of interacting with the pocket protein family. We show that HBP1 can interact with one of these, RB, both in vitro and in mammalian cells. Two distinct RB binding sites are present within HBP1--a high affinity binding site, mediated by an LXCXE motif and a separate low affinity binding site present within an activation domain. GAL4-fusion experiments indicate that HBP1 contains a masked activation domain. Deletion of two independent N- and C-terminal inhibitor domains unmasks an activation domain which is 100-fold more active than the full length protein. The released activation capacity is repressed by RB, p130 and p107. In addition, E1A can repress the activity of HBP1 via conserved region 1 sequences in a manner independent of the CBP co-activator. We show by stable expression in NIH3T3 cells that HBP1 has the capacity to induce morphological transformation of cells in culture.

Links

PubMed Online version:10.1038/sj.onc.1201243

Keywords

3T3 Cells; Adenovirus E1A Proteins/metabolism; Animals; High Mobility Group Proteins/metabolism; Humans; Mice; Phosphoproteins/metabolism; Protein Binding; Proteins; Repressor Proteins/metabolism; Retinoblastoma-Like Protein p130; Tumor Cells, Cultured

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


See also

References

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