Publication Date:
1996-05-31
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seol, W -- Choi, H S -- Moore, D D -- DK46546/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1336-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650544" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
DAX-1 Orphan Nuclear Receptor
;
DNA/*metabolism
;
DNA-Binding Proteins/chemistry/metabolism
;
Humans
;
Mice
;
Molecular Sequence Data
;
Receptors, Cytoplasmic and Nuclear/chemistry/*metabolism
;
Receptors, Retinoic Acid/chemistry/metabolism
;
Receptors, Thyroid Hormone/metabolism
;
Recombinant Fusion Proteins/chemistry/metabolism
;
*Repressor Proteins
;
Retinoid X Receptors
;
Signal Transduction
;
Transcription Factors/chemistry/metabolism
;
Transcriptional Activation/drug effects
;
Tumor Cells, Cultured
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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