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Volume 271, Number 31, Issue of August 2, 1996 pp. 18350-18354
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Formation of STAT5-containing DNA Binding Complexes in Response to Colony-stimulating Factor-1 and Platelet-derived Growth Factor

(Received for publication, April 5, 1996, and in revised form, May 15, 1996)

Ulrike Novak , Alice Mui ^¶ , Atsushi Miyajima and Lucy Paradiso

From the  University of Melbourne, Department of Medicine, Royal Melbourne Hospital, Parkville 3050, Australia, the ^¶ Department of Cell Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304-1104, and the  Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

Colony-stimulating factor (CSF-1) activates several members belonging to the STAT (signal transducers and activators of transcription) family of transcription factors. We investigated the DNA binding complexes activated by CSF-1 in several cell lines and compared them with complexes activated by platelet-derived growth factor and interleukin 3. Our results indicate that the SIF-A complex activated by CSF-1 and platelet-derived growth factor may contain STAT3/STAT5 heterodimers binding to the high affinity SIF binding site, m67. In addition, both growth factors activate one or several STAT5-containing protein complexes binding to the prolactin-inducible element, PIE. The formation of these complexes was cell type and growth factor specific. Interleukin 3 activated only PIE binding complexes containing STAT5A and STAT5B and did not activate m67 binding complexes. It appears, therefore, that STAT5 cannot bind to m67 as a homodimer, but it can bind if it is dimerized with STAT3, whereas it can bind to the PIE element without being either complexed with STAT3 or any other known STAT protein, possibly as a homodimer or as STAT5A/STAT5B heterodimer. However, in addition, STAT5 may heterodimerize with other proteins and form novel PIE binding complexes.

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