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Blood, 1 October 2005, Vol. 106, No. 7, pp. 2534-2542. Prepublished online as a Blood First Edition Paper on May 31, 2005; DOI 10.1182/blood-2004-06-2413. This Article Full Text (PDF) All Versions of this Article: 2004-06-2413v1 106/7/2534    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Shimokawa, T. Articles by Ra, C. Search for Related Content PubMed PubMed Citation Articles by Shimokawa, T. Articles by Ra, C. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted June 28, 2004 Accepted May 18, 2005 C/EBP functionally and physically interacts with GABP to activate the human myeloid IgA Fc receptor (FcR, CD89) promoter Toshibumi Shimokawa and Chisei Ra* Division of Molecular Cell Immunology and Allergology, Advanced Medical Research Center, Nihon University Graduate School of Medical Sciences, Tokyo, Japan * Corresponding author; email: fcericra{at}med.nihon-u.ac.jp. Human FcR (CD89), the Fc receptor for IgA, is expressed exclusively in myeloid cells, including granulocytes and monocytes/macrophages, and considered to define a crucial role of these cells in immune and inflammatory responses. A 259-base pair fragment of the FcR promoter is sufficient to direct myeloid expression of a reporter gene, and contains functionally important binding sites for C/EBP (CE1, CE2, and CE3) and an unidentified Ets-like nuclear protein. Here, we showed that the Ets-binding site is bound by a heterodimer composed of GABP, an Ets-related factor, and GABP, a Notch-related protein. Co-transfection of GABP increased FcR promoter activity 3.7 fold through the Ets-binding site. GABP and C/EBP synergistically activated the FcR promoter 280 fold. Consistent with these observations, in vitro binding analyses revealed a physical interaction between the GABP subunit and C/EBP. This is the first report demonstrating both physical and functional interactions between the GABP and C/EBP, and will provide new insights into the molecular basis of myeloid gene expression. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C. B. Lai, Y. Zhang, S. L. Rogers, and D. L. Mager Creation of the two isoforms of rodent NKG2D was driven by a B1 retrotransposon insertion Nucleic Acids Res., May 1, 2009; 37(9): 3032 - 3043. [Abstract] [Full Text] [PDF] M. Yaneva, S. Kippenberger, N. Wang, Q. Su, M. McGarvey, A. Nazarian, L. Lacomis, H. Erdjument-Bromage, and P. Tempst PU.1 and a TTTAAA Element in the Myeloid Defensin-1 Promoter Create an Operational TATA Box That Can Impose Cell Specificity onto TFIID Function. J. Immunol., June 1, 2006; 176(11): 6906 - 6917. [Abstract] [Full Text] [PDF]

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