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This version published online on December 6, 2005
Journal of Clinical Endocrinology & Metabolism, doi:10.1210/jc.2004-1957
A more recent version of this article appeared on February 1, 2006
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Submitted on October 11, 2004
Accepted on November 23, 2005

Identification and Characterization of Two Novel Splicing Isoforms of Human ERR{beta}

Wei Zhou, Zhilin Liu, Jianbo Wu, Jinghua Liu, Salman M. Hyder, Eric Antoniou, and Dennis B. Lubahn*

Departments of Biochemistry, Animal Sciences, Dalton Cardiovascular Research Center and Department of Biomedical Sciences, Child Health, MU Center for Phytonutrient and Phytochemical Studies, University of Missouri, Columbia, MO 65211

* To whom correspondence should be addressed. E-mail: LubahnD{at}missouri.edu.

Context: Estrogen-related receptor {beta} (ERR{beta}) was one of the first two orphan nuclear receptors reported and is believed to play important roles in estrogen-regulated pathways. Embryo lethality of ERR{beta} null mice indicated that ERR{beta} is essential for embryo development.

Objective: Two novel splicing isoforms of human ERR{beta}: hERR{beta}2-{Delta}10 and Short-form hERR{beta} were identified during the cloning of previously reported human ERR{beta}-hERR{beta}2. We aim to investigate the functional differences of these three human ERR{beta} splicing isoforms.

Results and Conclusions: A genomic sequence comparison within and flanking the ERR{beta} genes of eight species demonstrated that Short-form hERR{beta} lacks an F domain and is the matched homolog of mouse and rat ERR{beta} proteins in human. However, hERR{beta}2-{Delta}10 and the previously reported hERR{beta}2 isoforms are primate specific. RT-PCR analysis showed that Short-form hERR{beta} has a wide distribution in the 24 out of 27 human tissues and cell lines tested, while hERR{beta}2 and hERR{beta}2-{Delta}10 were only expressed in testis and kidney. The three human ERR{beta} splicing isoforms have different transcriptional activities when measured on an ERE-driven luciferase reporter in transfection assays. The localization of a nuclear localization signal (NLS) of Short-form hERR{beta} was also determined. Interestingly, the F domain of hERR{beta}2 alters the function of the NLS. Therefore, the ERR{beta} isoforms are likely to have diverse biological functions in vivo and characterizing the three isoforms of ERR{beta} will lead to an understanding of the multiple levels of gene regulation involved in steroid-receptor-signaling pathways in humans and may provide novel therapeutic targets for human diseases.
Key words: estrogen-related receptor beta (ERR{beta}) • orphan nuclear receptor • splicing isoform • tissue-specific • estrogen response element (ERE) • F domain • NLS (nuclear localization signal)




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