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Molecular and Cellular Biology, February 1999, p. 1049-1055, Vol. 19, No. 2
Institute of Molecular and Cellular
Biosciences,
Received 20 July 1998/Returned for modification 8 September
1998/Accepted 6 November 1998
The nuclear vitamin D receptor (VDR) is a member of a nuclear
receptor superfamily and acts as a ligand-dependent transcription factor. A family of cotranscriptional activators (SRC-1, TIF2, and
AIB-1) interacts with and activates the transactivation function of
nuclear receptors in a ligand-dependent way. We examined interaction of
VDR with these coactivators that was induced by several vitamin D
analogs, since they exert differential subsets of the biological action
of vitamin D through unknown mechanisms. Unlike other vitamin D analogs
tested, OCT (22-oxa-1
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Selective Interaction of Vitamin D Receptor with Transcriptional
Coactivators by a Vitamin D Analog
,25-dihydroxyvitamin
D3) induced interaction of VDR with TIF2 but not with SRC-1
or AIB-1. Consistent with these interactions, only TIF2 was able to
potentiate the transactivation function of VDR bound to OCT. Thus, the
present findings suggest that the structure of VDR is altered in a
vitamin D analog-specific way, resulting in selective interactions of VDR with coactivators. Such selective interaction of coactivators with
VDR may specify the array of biological actions of a vitamin D analog
like OCT, possibly through activating a particular set of target gene promoters.
*
Corresponding author. Mailing address: Institute of
Molecular and Cellular Biosciences, The University of Tokyo,
Yayoi 1-1-1, Bunkyo-ku, Tokyo 113, Japan. Phone:
81-3-5802-8632. Fax: 81-3-5684-8342. E-mail:
uskato{at}hongo.ecc.u-tokyo.ac.jp.
Molecular and Cellular Biology, February 1999, p. 1049-1055, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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