An Orphan Nuclear Hormone Receptor That Lacks a DNA Binding Domain and Heterodimerizes with Other Receptors
SciencePublished 31 May 1996
Wongi Seol, Hueng-Sik Choi, David D. Moore
Citations538
SJR quartileQ1
SJR score10.42
SNIP6.62
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TL;DR
In mammalian cells, SHP specifically inhibited transactivation by the superfamily members with which it interacted, suggesting that SHP functions as a negative regulator of receptor-dependent signaling pathways.
Abstract
SHP is an orphan member of the nuclear hormone receptor superfamily that contains the dimerization and ligand-binding domain found in other family members but lacks the conserved DNA binding domain. In the yeast two-hybrid system, SHP interacted with several conventional and orphan members of the receptor superfamily, including retinoid receptors, the thyroid hormone receptor, and the orphan receptor MB67. SHP also interacted directly with these receptors in vitro. In mammalian cells, SHP specifically inhibited transactivation by the superfamily members with which it interacted. These results suggest that SHP functions as a negative regulator of receptor-dependent signaling pathways.
Keywords
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