Journal article
A Novel Zinc Finger Transcription Factor with Two Isoforms That Are Differentially Repressed by Estrogen Receptor-α
The Journal of biological chemistry, Vol.277(11), pp.9326-9334
03/15/2002
DOI: 10.1074/jbc.M107702200
PMID: 11779858
Abstract
Estrogen receptor-α (ERα) can induce the expression of genes in response to estrogen by binding to estrogen response elements in the promoters of target genes. There is growing evidence that ERα can alter patterns of gene expression in response to ligand by regulating the activity of other factors through a direct protein-protein interaction. To identify other factors that are regulated by ERα, a yeast two-hybrid screen was performed that identified a novel Cys2His2 zinc finger protein named ZER6. The ZER6 protein contains a Kruppel-associated box domain and six Cys2His2 zinc fingers. Transcripts from theZER6 gene can have alternate 5′ exons and encode either a p71 or p52 isoform. The p52-ZER6 protein interacts strongly with ERα in the presence of 17β-estradiol, whereas the p71-ZER6 isoform has a HUB-1 amino-terminal domain that inhibits the interaction with ERα. A consensus ZER6 binding element was defined using PCR-assisted binding site selection. In COS-1 cells, both the p52 and p71 isoforms can activate transcription through the ZER6 binding element; however, in the presence of ERα, transactivation by the p52 isoform is specifically repressed. Overexpression of the p52 isoform was able to abrogate activation by p71-ZER6. Expression of ZER6 was largely restricted to the mammary gland with a lower level of expression in the kidney. We conclude that ZER6 is a novel zinc finger transcription factor in which regulation of transcription in hormone-responsive cells can be controlled by the relative level of expression of two distinct isoforms.
Details
- Title: Subtitle
- A Novel Zinc Finger Transcription Factor with Two Isoforms That Are Differentially Repressed by Estrogen Receptor-α
- Creators
- Andrew T. Conroy - Stanford UniversityManju Sharma - Stanford UniversityAnn E. Holtz - Stanford UniversityChengbiao Wu - Stanford UniversityZijie Sun - Stanford UniversityRonald J. Weigel - Stanford University
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.277(11), pp.9326-9334
- DOI
- 10.1074/jbc.M107702200
- PMID
- 11779858
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 03/15/2002
- Academic Unit
- Molecular Physiology and Biophysics; Anatomy and Cell Biology; Surgery; Biochemistry and Molecular Biology
- Record Identifier
- 9984284349702771
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