An Orphan Nuclear Hormone Receptor That Lacks a DNA Binding Domain and Heterodimerizes with Other Receptors

@article{Seol1996AnON,  title={An Orphan Nuclear Hormone Receptor That Lacks a DNA Binding Domain and Heterodimerizes with Other Receptors},  author={Wongi Seol and Hueng-Sik Choi and David D. Moore},  journal={Science},  year={1996},  volume={272},  pages={1336 - 1339},  url={https://api.semanticscholar.org/CorpusID:32853062}}
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.

546 Citations

Novel receptor interaction and repression domains in the orphan receptor SHP

The results identify novel receptor interaction and repressor domains in SHP and suggest two distinct mechanisms for inhibition of receptor signaling pathways by SHP.

The Orphan Nuclear Receptor SHP Inhibits Agonist-dependent Transcriptional Activity of Estrogen Receptors ERα and ERβ*

It is shown here that SHP interacts directly with agonist-bound estrogen receptors, ERα and ERβ, and inhibits ER-mediated transcriptional activation, and suggests that competition for coactivator-binding is a novel mechanism by which SHP may inhibit nuclear receptor activation.

Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner).

It is shown that SHP also interacts with estrogen receptors and inhibits their function, suggesting that it functions to regulate estrogen signaling through a direct interaction with ERalpha.

The Orphan Nuclear Receptor SHP Utilizes Conserved LXXLL-Related Motifs for Interactions with Ligand-Activated Estrogen Receptors

It is demonstrated that SHP variants, carrying either interaction-defective NR box mutations or a deletion of the repressor domain, have lost the capacity to inhibit agonist-dependent transcriptional estrogen receptor activation, and studies indicate that SHp may function as a cofactor via the formation of ternary complexes with dimeric receptors on DNA.

Activation of the Promoter of the Orphan Receptor SHP by Orphan Receptors That Bind DNA as Monomers*

The results suggest that alterations in the levels or activities of SF-1 or FTF could modulate SHP expression in appropriate tissues and thereby affect a variety of receptor dependent signaling pathways.

Molecular mechanisms of transcriptional repression by the orphan receptor SHP

This thesis investigates the molecular mechanisms of the transcriptionally inhibitory effect of SHP, and suggests that EID-family members act as inhibitors of p300/CBP-dependent transcription in a tissue-specific manner and histone acetyltransferases and histones as targets for EID1 action.

Differential Regulation of the Orphan Nuclear ReceptorSmall Heterodimer Partner (SHP) Gene Promoter by Orphan Nuclear Receptor ERR Isoforms*

The results identify a new autoregulatory loop controlling SHP gene expression and significantly extend the potential functional roles of the three ERRs.

The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity.

It is demonstrated that SHP is able to interact with LXR and to modulate its transcriptional activity, as demonstrated by glutathione-S-transferase pull-down assays, mammalian two-hybrid, and coimmunoprecipitation experiments.
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35 References

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Yeast two-hybrid system identifies a protein, thyroid hormone receptor uncoupling protein (TRUP), that specifically interacts with a region of the human thyroid hormone receptors consisting of the hinge region and the N-terminal portion of the ligand binding domain in a hormone-independent manner.

Interaction of thyroid-hormone receptor with a conserved transcriptional mediator

It is shown that Tripl can functionally substitute for Sugl in yeast, and that both proteins interact in vitro with the thyroid-hormone receptor, and with the transcriptional activation domains of yeast GAL4 and of herpes virus VP16.

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It is demonstrated that both HRE binding and the transcriptional inducing activities of one member of this family, TH receptor, were markedly enhanced by heterodimerization with H-2RIIBP, a non-TH-binding member of the steroid hormone receptor superfamily.

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It is proposed that MB67 plays an important role in the complex network of proteins that govern response to retinoic acid and its metabolites.

Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily

Results indicate that SRC-1 encodes a coactivator that is required for full transcriptional activity of the steroid receptor superfamily.

The orphan receptors NGFI-B and steroidogenic factor 1 establish monomer binding as a third paradigm of nuclear receptor-DNA interaction

A common mechanism of NGFI-B and SF-1 DNA binding is defined, which may underlie a competitive mechanism of gene regulation in steroidogenic tissues that express these proteins.

Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α

The crystal structure of the human retinoid-X receptor RXR-α ligand-binding domain reveals a previously undiscovered fold of an antiparallel α-helical sandwich, packed as dimeric units. Two helices…

Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors.

In cotransfections, neither RIP14 nor RIP15 trans-activates a reporter containing multiple copies of the beta RARE under any of a variety of conditions, suggesting that their activities are dependent on the binding of as yet unidentified specific ligands or on activation by other processes.

RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors.

It is shown that recombinant RAR and T3R are monomers in solution and cannot form stable homodimeric complexes on their responsive elements.

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