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Blood, 15 September 2000, Vol. 96, No. 6, pp. 2233-2239
NEOPLASIA
Ligand-inducible interaction of the DRIP/TRAP coactivator complex
with retinoid receptors in retinoic acid-sensitive and -resistant
acute promyelocytic leukemia cells
Wenlin Shao,
Angelika Rosenauer,
Koren Mann,
Chao-Pei Betty Chang,
Christophe Rachez,
Leonard P. Freedman, and
Wilson H. Miller Jr
From the Department of Medicine, Division of
Experimental Medicine, Lady Davis Institute for Medical Research, Sir
Mortimer B. Davis Jewish General Hospital, McGill University, Montreal,
Quebec, Canada; and the Cell Biology Program, Memorial Sloan-Kettering
Cancer Center, Sloan-Kettering Division, Graduate School of Medical
Sciences, Cornell University, New York, NY.
Retinoic acid (RA) signaling is mediated by its nuclear
receptors RXR and RAR, which bind to their cognate response elements as
a heterodimer, RXR/RAR, and act in concert with coregulatory factors to
regulate gene transcription on ligand binding. To identify specific
cofactors that interact with the RXR/RAR heterodimer in acute
promyelocytic leukemia (APL) cells, a double cistronic construct was
used that allowed coexpression of the RXR LBD (ligand binding domain)
with the RAR LBD as an affinity matrix to pull down interacting
proteins from nuclear extracts prepared from a human APL cell line,
NB4. A group of proteins was detected whose interaction with RXR/RAR is
ligand inducible. The molecular weight pattern of these proteins is
similar to that of a complex of proteins previously identified as DRIP
or TRAP, which are ligand-dependent transcription activators of VDR and
TR, respectively. The RXR/RAR-interacting proteins from NB4 were
confirmed to be identical to the DRIP subunits by comparative
electrophoresis, Western blot analysis, and in vitro protein
interaction assay. In addition to RXR/RAR, the DRIP component can
interact directly with the APL-specific PML-RAR fusion protein. The
same DRIP complex is present in RA-resistant APL cells and in a variety
of cancer cell lines, supporting its global role in transcriptional regulation.
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