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This version published online on February 12, 2004
Molecular Endocrinology, doi:10.1210/me.2003-0339
Molecular Endocrinology Vol. 0, No. 2004 200303391-
doi:10.1210/me.2003-0339
Copyright © 2004 by the Endocrine Society.
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*Genetics Home Reference

Submitted on September 5, 2003
Accepted on February 5, 2004

Differential role of the loop region between helices H6 and H7 within the orphan nuclear receptors SHP and DAX-1

Yun-Yong Park, Han-Jong Kim, Joon-Young Kim, Mi-Young Kim, Kwang-Hoon Song, Ki Cheol Park, Kang-Yeol Yu, Minho Shong, Kyoung-Hee Kim, and Hueng-Sik Choi*

Hormone Research Center, School of Biological Sciences and Technology, Chonnam National University, Gwangju, 500-757, Republic of Korea; KOMED Institute for Life Science, Graduate School of Biotechnology, Korea University, Seoul, Republic of Korea; Laboratory of Endocrine Cell Biology, Department of Internal Medicine, Chungnam National University School of Medicine, Daejon, Republic of Korea; R&D Park, LG Life Sciences, Ltd, Daejeon, 305-380, Republic of Korea

* To whom correspondence should be addressed. E-mail: hsc{at}chonnam.chonnam.ac.kr.

The orphan nuclear receptors SHP and DAX-1 contain extra amino acids between helices H6 and H7 of LBD and here we investigated a possible role of these additional amino acids. Transient transfection assay demonstrated that in contrast to wild type, mutant SHP {Delta}28-139, deletion of 12 extra amino acids in H6-H7, failed to repress the transactivity of orphan nuclear receptors such as ERR{gamma}, HNF4{alpha}and CAR. Interestingly, yeast-two hybrid and GST-pull down assays demonstrated that wild type and SHP {Delta}28-139 have similar abilities to interact with ERR{gamma}, HNF4{alpha}and mCAR. Unexpectedly, wild type DAX-1 and mutant DAX-1 {Delta}38-362, deletion of 25 extra amino acids in H6-H7, had no significant difference in the interaction and repression of SF-1 transactivation. Mutant SHP that contains DAX-1 extra amino acids or poly-alanine stretch in H6-H7 showed indistinguishable pattern of repression from wild type SHP. Interestingly, the swapped SHP mutant with DAX-1 extra amino acids interacted with EID-1, which is characterized as an SHP interacting corepressor. However, interaction between SHP {Delta}28-139 and EID-1 was significantly diminished. Moreover, SHP-mediated repression of mCAR transactivation was significantly released by down-regulation of EID-1 expression with EID-1 siRNA. The present study suggests that H6-H7 loop regions of SHP and DAX-1 play a different role in the repression of nuclear receptor transactivation.
Key words: orphan nuclear receptor • transcriptional repression • SHP • DAX-1 • EID-1

NURSA Molecule Pages Link:

Nuclear Receptors:   DAX1  |  SHP  |  CAR  |  HNF4α  |  ERRγ  |  SF-1  |  LRH-1
Coregulators:   SRC-1



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