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ATF-2 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, ATF-2 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 ATF-2
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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