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Division of Molecular Endocrinology (C.A.P., M.M., B.M.R., H.H.S.) Departments of Medicine (D.R., M.M., B.M.R., H.H.S.), Cell Biology (D.R.), and Pharmacology (M.M., B.M.R., H.H.S.) Skirball Institute of Biomolecular Medicine (D.R.) New York University Medical Center New York, New York 10016
Nuclear receptors for steroid hormones, thyroid
hormone, retinoids, and vitamin D are thought to mediate their
transcriptional effects in concert with coregulator proteins that
modulate receptor interactions with components of the basal
transcription complex. In an effort to identify potential coregulators,
receptor fusions with glutathione-S-transferase were
used to isolate proteins in nuclear extracts capable of binding nuclear
hormone receptors. Glutathione-S-transferase fusions with
mouse retinoid X receptor-
enabled the selective isolation of a
65-kDa protein (p65) from nuclear extracts of rat and human cells.
Binding of p65 to mouse retinoid X receptor- was centered around the
DNA-binding domain. p65 also bound regions encompassing the DNA-binding
domain in estrogen, thyroid hormone, and glucocorticoid receptors. p65
was identified as TLS (translocated-in-liposarcoma), a recently
identified member of the RNP family of nuclear RNA-binding proteins
whose members are thought to function in RNA processing. The N-terminal
half of TLS bound to thyroid hormone receptor with high affinity while
the receptor was bound to appropriate DNA target sites. Functional
studies indicated that the N-terminal half of TLS can interact with
thyroid hormone receptor in vivo. TLS was originally
discovered as part of a fusion protein arising from a chromosomal
translocation causing human myxoid liposarcomas. TLS contains a potent
transactivation domain whose translocation-induced fusion with a
DNA-binding protein (CHOP) yields a powerful transforming oncogene and
transcription factor. The transactivation and RNA-binding properties of
TLS and the nature of its interaction with nuclear receptors
suggest a novel role in nuclear receptor function.
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