Interaction and functional cooperation of PEBP2/CBF with Smads - Synergistic induction of the immunoglobulin germline C alpha promoter
- Authors
- Hanai J; Chen LF; Kanno T; Ohtani-Fujita N; Kim WY; Guo WH; Imamura T; Ishid.ou Y; Fukuchi M; Shi MJ; Stavnezer J; Kawabata M; Miyazono K; Ito Y
- Issue Date
- Oct-1999
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY, v.274, no.44, pp 31577 - 31582
- Pages
- 6
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Volume
- 274
- Number
- 44
- Start Page
- 31577
- End Page
- 31582
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/150014
- DOI
- 10.1074/jbc.274.44.31577
- ISSN
- 0021-9258
1083-351X
- Abstract
- Smads are signal transducers for members of the transforming growth factor-beta (TGF-beta) superfamily. Upon ligand stimulation, receptor-regulated Smads (R-Smads) are phosphorylated by serine/threonine kinase receptors, form complexes with common-partner Smad, and translocate into the nucleus, where they regulate the transcription of target genes together with other transcription factors. Polyomavirus enhancer binding protein 2/core binding factor (PEEP2/CBF) is a transcription factor complex composed of alpha and beta subunits. The alpha subunits of PEEP2/CBF, which contain the highly conserved Hunt domain, play essential roles in hematopoiesis and osteogenesis. Here we show that three mammalian alpha subunits of PEBP2/CEF form complexes with R-Smads that act in TGF-beta/activin pathways as well as those acting in bone morphogenetic protein (BMP) pathways. Among them, PEBP2 alpha C/CBFA3/AML2 forms a complex with Smads and stimulates transcription of the germline Ig C alpha promoter in a cooperative manner, for which binding of both factors to their specific binding sites is essential. PEEPS may thus be a nuclear target of TGF-beta/BMP signaling.
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