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Type I Receptor in Vivo
(Received for publication, July 2, 1996)
,
,
,
,
and§
From the The type I transforming growth factor-
Department of Biochemistry, The Cancer
Institute, Tokyo, Japanese Foundation for Cancer Research, 1-37-1 Kami-Ikebukuro, Toshima-ku, Tokyo 170, Japan and § The
Vanderbilt Cancer Center, Nashville, Tennessee 37232
receptor (TR-I) is the efferent component of the receptor complex,
which presumably phosphorylates intracellular targets. FKBP12, a
binding protein for FK506 and rapamycin, is shown to associate with the
cytoplasmic region of TR-I in vitro. In this report, we
investigated the interaction of FKBP12 with TR-I in
vivo. FKBP12 interacts with TR-I in mammalian cells as well as
in yeast. Ligand addition does not affect the interaction, and both
constitutively active and kinase-negative mutants of TR-I bind
FKBP12. FKBP12 dissociates from TR-I in the presence of a high
concentration of FK506. The juxtamembrane region of TR-I, containing
the major phosphorylation sites by the type II receptor, is required
for the interaction. One of the deletion mutants in this region, which
was shown to mediate transcriptional response, does not bind FKBP12,
suggesting that FKBP12 is not directly involved in TGF- signaling.
Furthermore TR-I does not phosphorylate FKBP12 in vitro.
FKBP12 may not be a direct substrate of TR-I but possibly modulates
the TR-I function through its interaction with the regulatory domain
of the kinase.
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