Abstract
The functional characterization of ETS transcription factors have allowed the association of numerous physiological and pathological roles to these proteins in the regulation of gene expression during the maturation of hematopoietic cell lineages and in tumor cell growth, invasion, and metastasis. Moreover, structural investigations have allowed the determination of certain amino acid domains of ETS proteins that are essential for the recognition and transcriptional activation or repression of gene promoters or enhancers. It has been observed that the mechanisms of action of ETS proteins can be ruled in part by their intermolecular interactions with other transcription factors and by their phosphorylation status. This review describes information about structure-function relationships of different ETS family members in order to establish the structural differences that are important for their affinities and intrinsic activities to DNA binding sites.
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