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Division of Endocrinology (G.B.A., X.H., M.G.G., M.A.L.),
Diabetes, and Metabolism Departments of Medicine and Genetics,
and The Penn Diabetes Center University of Pennsylvania School
of Medicine Philadelphia, Pennsylvania 19104
Cell Biology
Program (C.R., L.P.F.) Memorial Sloan-Kettering Cancer Center
New York, New York 10021
A mutation in the nuclear orphan receptor ROR
results in a severe impairment of cerebellar development by unknown
mechanisms. We have shown previously that ROR contains a strong
constitutive activation domain in its C terminus. We therefore searched
for mammalian ROR coactivators using the minimal activation domain
as bait in a two-hybrid screen. Several known and putative coactivators
were isolated, including glucocorticoid receptor-interacting protein-1
(GRIP-1) and peroxisome proliferator-activated receptor (PPAR)-binding
protein (PBP/TRAP220/DRIP205). These interactions were confirmed
in vitro and require the intact activation domain of ROR
although different requirements for interaction with GRIP-1 and PBP
were detected. Even in the absence of exogenous ligand, ROR
interacts with a complex or complexes of endogenous proteins, similar
to those that bind to ligand-occupied thyroid hormone and vitamin D
receptors. Both PBP and GRIP-1 were shown to be present in these
complexes. Thus we have identified several potential ROR
coactivators that, in contrast to the interactions with hormone
receptors, interact with ROR in yeast, in bacterial extracts, and in
mammalian cells in vivo and in vitro in the
absence of exogenous ligand. GRIP-1 functioned as a coactivator for the
ROR both in yeast and in mammalian cells. Thus, GRIP-1 is the first
proven coactivator for ROR.
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