Dimer formation by ternary complex factor ELK-1

Ternary complex factors (TCFs), a subgroup of the ets protein family, bind with a dimer of serum response factor to the c-fos serum response element. Both DNA binding and transcriptional activation by TCFs are regulated by mitogen-activated protein kinases. When activated, mitogen-activated protein kinases form homodimers that translocate to the nucleus, where they interact with TCFs via specific docking sites. Here we show by three different criteria that Elk-l is capable of forming dimers in eukaryotic cells through two distinct interaction domains. These observations are consistent with a dynamic model of TCF-promoter interactions.