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(Received for publication, February 6, 1996)
From the Departments of Cellular and Molecular Pharmacology, and
Biochemistry and Biophysics, University of California, San
Francisco, San Francisco, California 94143-0448
Steroid hormones bind and activate intracellular
receptors that are ligand-regulated transcription factors. Mammalian
steroid receptors can confer hormone-dependent
transcriptional enhancement when expressed in yeast, thereby enabling
the genetic identification of nonreceptor proteins that function in the
hormone signal transduction pathway. Pdr5p (Lem1/Sts1/Ydr1p), a yeast
ATP-binding cassette transporter, selectively decreases the
intracellular levels of particular steroid hormones, indicating that
active processes can affect the passage of steroids across biological
membranes. In yeast, the immunosuppressive drug FK506 inhibited Pdr5p,
thereby potentiating activation of the glucocorticoid receptor by
dexamethasone, a ligand that is exported by Pdr5p. In mammalian L929
cells but not in HeLa cells, FK506 potentiated dexamethasone
responsiveness and increased dexamethasone accumulation, without
altering the hormone-binding properties of the glucocorticoid receptor.
We suggest that an FK506-sensitive transporter in L929 cells
selectively decreases intracellular hormone levels and, consequently,
the potency of particular steroids. Thus, steroid transporters may
modulate, in a cell-specific manner, an initial step in signaling, the
availability of hormone to the receptor.
Volume 271, Number 29,
Issue of July 19, 1996
pp. 17152-17156
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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