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 Blood, 15 May 2007, Vol. 109, No. 10, pp. 4209-4219.
Prepublished online as a Blood First Edition Paper on January 25, 2007; DOI 10.1182/blood-2005-09-031963.

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HEMATOPOIESIS

Modulation of DNA binding properties of CCAAT/enhancer binding protein epsilon by heterodimer formation and interactions with NFkappaB pathway

Alexey M. Chumakov1, Agnes Silla1, Elizabeth A. Williamson2, and H. Phillip Koeffler1

1 Department of Medicine, Hematology/Oncology, Cedars-Sinai Medical Center and the Department of Pathology and Laboratory Medicine, University of California at Los Angeles; 2 University of New Mexico Cancer Research Facility, Albuquerque

C/EBP epsilon is a transcription factor involved in myeloid cell differentiation. Along with C/EBP-{alpha}, -ß, -{gamma}, -{delta}, and -{zeta}, C/EBP-{epsilon} belongs to the family of CCAAT/enhancer binding proteins that are implicated in control of growth and differentiation of several cell lineages in inflammation and stress response. We have previously shown that C/EBP-{epsilon} preferentially binds DNA as a heterodimer with other C/EBP family members such as C/EBP-{delta}, CHOP (C/EBP-{zeta}), and the b-zip family protein ATF4. In this study, we define the consensus binding sites for C/EBP-{epsilon} dimers and C/EBP-{epsilon}–ATF4 heterodimers. We show that the activated NFkappaB pathway promotes interaction of the C/EBP-{epsilon} subunit with its cognate DNA binding site via interaction with RelA. RelA-C/EBP interaction is enhanced by phosphorylation of threonine at amino acid 75 and results in increased DNA binding compared with the wild-type nonphosphorylated C/EBP both in vitro and in vivo. We suggest that interaction of the activated NFkappaB pathway and C/EBP-{epsilon} may be important in selective activation of a subset of C/EBP-{epsilon}–responsive genes.


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