Abstract
Thyroid hormone receptors (TRs) and the oncoprotein v-erbA can heterodimerize with retinoid X receptor (RXR) on core motifs arranged as inverted repeats (IR0) which contain the consensus sequence AGGTCA. On this core motif, v-erbA can also form homodimers whereas TRs homodimerize very poorly. Therefore to obtain a better understanding of distinct homodimerization properties of TRα1 as compared to those of v-erbA, we created chimeras between these two receptors and tested their abilities to homodimerize on IR0. We found that the enhanced homodimerization properties of v-erbA compared to those of TRα1 on IR0 map to amino acids 107–156 in v-erbA/121–170 in TRα1 (VT-2 chimera). Furthermore, functional studies on transient transfections showed that v-erbA–RXR heterodimers do not mediate the dominant negative activity of v-erbA on an inverted repeat response element. These data, in conjunction with our previous studies, indicate that v-erbA homodimers mediate the repressor activity of v-erbA on IR0.
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