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J Biol Chem, Vol. 275, Issue 18, 13510-13516, May 5, 2000
From the Department of Pathology, Northwestern University Medical
School, Chicago, Illinois 60611
We previously isolated and identified steroid
receptor coactivator-1 (SRC-1) and peroxisome proliferator-activated
receptor (PPAR)-binding protein (PBP/PPARBP) as coactivators for PPAR, using the ligand-binding domain of PPAR The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF216186.
Isolation and Characterization of Peroxisome
Proliferator-activated Receptor (PPAR) Interacting Protein (PRIP) as a
Coactivator for PPAR*
as bait in a yeast
two-hybrid screening. As part of our continuing effort to identify
cofactors that influence the transcriptional activity of PPARs, we now
report the isolation of a novel coactivator from mouse, designated PRIP (peroxisome proliferator-activated receptor
interacting protein), a nuclear protein with
2068 amino acids and encoded by 13 exons. Northern analysis showed that
PRIP mRNA is ubiquitously expressed in many tissues of adult mice.
PRIP contains two LXXLL signature motifs. The
amino-terminal LXXLL motif (amino acid position 892 to 896)
of PRIP was found to be necessary for nuclear receptor interaction, but
the second LXXLL motif (amino acid position 1496 to 1500)
appeared unable to bind PPAR. Deletion of the last 12 amino acids
from the carboxyl terminus of PPAR resulted in the abolition of the
interaction between PRIP and PPAR. PRIP also binds to PPAR
,
RAR, RXR, ER, and TR
1, and this binding is increased in the
presence of specific ligands. PRIP acts as a strong coactivator for
PPAR in the yeast and also potentiates the transcriptional
activities of PPAR and RXR in mammalian cells. A truncated form
of PRIP (amino acids 786-1132) acts as a dominant-negative repressor,
suggesting that PRIP is a genuine coactivator.
*
This work was supported by National Institutes of Health
Grants R37 GM23750 (to J. K. R.) and DK28492 (to Y. S. K.), by
Department of Veterans Affairs merit review grants (to A. V. Y. and
M. S. R.), and by the Joseph L. Mayberry, Sr. Endowment Fund. This
work was presented at the Keystone Symposium on PPARs in April 1999.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Pathology,
Northwestern University Medical School, 303 East Chicago Ave., Chicago,
IL 60611. Tel.: 312-503-7948; Fax: 312-503-8249; E-mail: jkreddy@nwu.edu.
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Y. Zhu, C. Qi, W.-Q. Cao, A. V. Yeldandi, M. Sambasiva Rao, and J. K. Reddy Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function PNAS, August 17, 2001; (2001) 181347498. [Abstract] [Full Text] [PDF]
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S.-K. Lee, S.-Y. Jung, Y.-S. Kim, S.-Y. Na, Y. C. Lee, and J. W. Lee Two Distinct Nuclear Receptor-Interaction Domains and CREB-Binding Protein-Dependent Transactivation Function of Activating Signal Cointegrator-2 Mol. Endocrinol., February 1, 2001; 15(2): 241 - 254. [Abstract] [Full Text]
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M. del Mar Gonzalez-Barroso, C. Pecqueur, C. Gelly, D. Sanchis, M.-C. Alves-Guerra, F. Bouillaud, D. Ricquier, and A.-M. Cassard-Doulcier Transcriptional Activation of the Human ucp1 Gene in a Rodent Cell Line. SYNERGISM OF RETINOIDS, ISOPROTERENOL, AND THIAZOLIDINEDIONE IS MEDIATED BY A MULTIPARTITE RESPONSE ELEMENT J. Biol. Chem., October 6, 2000; 275(41): 31722 - 31732. [Abstract] [Full Text] [PDF]
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Y. Zhu, C. Qi, W.-Q. Cao, A. V. Yeldandi, M. S. Rao, and J. K. Reddy Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function PNAS, August 28, 2001; 98(18): 10380 - 10385. [Abstract] [Full Text] [PDF]
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