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J. Biol. Chem., Vol. 275, Issue 43, 33201-33204, October 27, 2000
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with Transcriptional
Coactivators*
,§,,§,§, and§¶
From the The nuclear peroxisome proliferator-activated
receptor Institute of Molecular and Cellular
Biosciences, University of Tokyo, Tokyo 113-0032, Japan and the
§ Core Research for Evolutional Science and Technology,
Japan Science and Technology Corporation, Saitama 332-0012, Japan
(PPAR) is a member of the nuclear receptor superfamily
and acts as a ligand-dependent transcription factor
mediating adipocyte differentiation, cell proliferation and
inflammatory processes, and modulation of insulin sensitivity. Members
of the 160-kDa protein (SRC-1/TIF2/AIB-1) family of
coactivators, CBP/p300 and TRAP220/DRIP205, are shown to interact
directly with PPAR and potentiate nuclear receptor transactivation
function in a ligand-dependent fashion. Because PPAR
ligands exert partially overlapping but distinct subsets of biological
action through PPAR binding, we wished to examine whether
interactions between PPAR and known coactivators were induced to the
same extent by different classes of PPAR ligand. The natural ligand
15-deoxy-
12,14-prostaglandin J2 induced
PPAR interactions with all coactivators tested (SRC-1, TIF2, AIB-1,
p300, TRAP220/DRIP205) in yeast and mammalian two-hybrid assays, as
well as in a glutathione S-transferase pull-down
assay. However, under the same conditions troglitazone, a synthetic
PPAR ligand that acts as an antidiabetic agent, did not induce
PPAR interactions with any of the coactivators. Our findings suggest that ligand binding may alter PPAR structure in a ligand
type-specific way, resulting in distinct PPAR-coactivator interactions.
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