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J Biol Chem, Vol. 274, Issue 19, 12971-12974, May 7, 1999
Signaling through Smad
Proteins
,§,§, and§
From the Several lines of experiments demonstrated the
interplay between the transforming growth factor- Institute of Molecular and Cellular
Biosciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo
113-0034, Japan, § CREST, Japan Science and Technology,
4-1-8 Honcho, Kawaguchi, Saitama 332, Japan, and the ¶ Department
of Biochemistry, The Cancer Institute, Tokyo, Japanese Foundation for
Cancer Research, and Research for the Future Program, Japan Society for
the Promotion of Science, 1-37-1 Kami-Ikebukuro, Toshima-ku,
Tokyo 170-8455, Japan
(TGF-) and
vitamin D signaling pathways. Recently, we found that Smad3, a
downstream component of the TGF- signaling pathway, potentiates
ligand-induced transactivation of vitamin D receptor (VDR) as a
coactivator of VDR (Yanagisawa, J., Yanagi, Y., Masuhiro, Y., Suzawa,
M., Watanabe, M., Kashiwagi, K., Toriyabe, T., Kawabata, M., Miyazono,
K., and Kato, S. (1999) Science 283, 1317-1321). Here, we investigated the roles of inhibitory Smads, Smad6
and Smad7, which are negative regulators of the TGF-/bone morphogenetic protein signaling pathway, on the Smad3-mediated potentiation of VDR function. We found that Smad7, but not Smad6, abrogates the Smad3-mediated VDR potentiation. Interaction studies in vivo and in vitro showed that Smad7
inhibited the formation of the VDR-Smad3 complex, whereas Smad6 had no
effect. Taken together, our results strongly suggest that the interplay
between the TGF- and vitamin D signaling pathways is, at least in
part, mediated by the two classes of Smad proteins, which modulate VDR
transactivation function both positively and negatively.
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