ATF2 is a member of the group of bZip transcription factors. Heterodimer formation between members of the bZip group is common and is believed to add diversity to the cis-acting elements at which binding of the dimers is directed. Specifically, ATF2 may dimerize with c-Jun, as occurs in response to E1a, and in so doing shift the binding preference of c-Jun toward ATF/CRE sites (1-3). Deletion analysis has indicated that the N-terminal region of ATF2 containing threonine at residues 69 and 71 are essential for this purpose. These threonine residues are phosphorylated by JNK/SAPK for transcriptional activation.
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