BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation.

The c-Myc oncoprotein functions as a transcription factor that can transform normal cells into tumor cells, as well as playing a direct role in normal cell proliferation. The c-Myc protein transactivates cellular promoters by recruiting nuclear cofactors to chromosomal sites through an N-terminal transactivation domain. We have previously reported the ...
identification and functional characterization of four different c-Myc cofactors: TRRAP, hGCN5, TIP49, and TIP48. Here we present the identification and characterization of the actin-related protein BAF53 as a c-Myc-interacting nuclear cofactor that forms distinct nuclear complexes. In addition to the human SWI/SNF-related BAF complex, BAF53 forms a complex with TIP49 and TIP48 and a separate biochemically distinct complex containing TRRAP and a histone acetyltransferase which does not contain TIP60. Using deletion mutants of BAF53, we show that BAF53 is critical for c-Myc oncogenic activity. Our results indicate that BAF53 plays a functional role in c-Myc-interacting nuclear complexes.
Mesh Terms:
Acetyltransferases, Actins, Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Carrier Proteins, Cell Transformation, Neoplastic, Chromosomal Proteins, Non-Histone, DNA Helicases, DNA-Binding Proteins, Gene Deletion, Hela Cells, Histone Acetyltransferases, Histones, Humans, Mutation, Nuclear Proteins, Nucleosomes, Protein Binding, Proto-Oncogene Proteins c-myc, Saccharomyces cerevisiae Proteins, Transcription Factors
Mol. Cell. Biol.
Date: Mar. 01, 2002
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