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Published on: May 26, 2014
RBFOX2 protein domains and cellular activities
Anurada D Arya1, David I Wilson1, Diana Baralle1
1*Human Development and Health Academic Unit, Faculty of Medicine, University of Southampton, Institute of Developmental Sciences Building, Southampton General Hospital, Tremona Road, Southampton SO16 6YD, U.K.
Abstract:
RBFOX2 (RNA-binding protein, Fox-1 homologue 2)/RBM9 (RNA-binding-motif protein 9)/RTA (repressor of tamoxifen action)/HNRBP2 (hexaribonucleotide-binding protein 2) encodes an RNA-binding protein involved in tissue specific alternative splicing regulation and steroid receptors transcriptional activity. Its ability to regulate specific splicing profiles depending on context has been related to different expression levels of the RBFOX2 protein itself and that of other splicing regulatory proteins involved in the shared modulation of specific genes splicing. However, this cannot be the sole explanation as to why RBFOX2 plays a widespread role in numerous cellular mechanisms from development to cell survival dependent on cell/tissue type. RBFOX2 isoforms with altered protein domains exist. In the present article, we describe the main RBFOX2 protein domains, their importance in the context of splicing and transcriptional regulation and we propose that RBFOX2 isoform distribution may play a fundamental role in RBFOX2-specific cellular effects.
Insights
RBFOX2 protein regulates gene splicing and transcription. Its diverse cellular roles may stem from different RBFOX2 protein isoforms, not just expression levels.
Area of Science:
- Molecular Biology
- Genetics
- Cell Biology
Background:
- RBFOX2 (RNA-binding protein, Fox-1 homologue 2) is an RNA-binding protein.
- It regulates tissue-specific alternative splicing and steroid receptor transcriptional activity.
- Its widespread cellular roles suggest mechanisms beyond simple expression level changes.
Purpose of the Study:
- To describe the main RBFOX2 protein domains.
- To explain their importance in splicing and transcriptional regulation.
- To propose that RBFOX2 isoform distribution influences its specific cellular effects.
Main Methods:
- Literature review of RBFOX2 protein domains.
- Analysis of RBFOX2's role in splicing and transcription.
- Hypothesis generation on isoform function.
Main Results:
- RBFOX2 protein domains are crucial for its regulatory functions.
- Existing explanations based on expression levels are insufficient.
- RBFOX2 isoforms with altered domains exist.
Conclusions:
- RBFOX2 protein domains are key to its functions.
- RBFOX2 isoform distribution is proposed as a critical factor in its cellular specificity.
- Further research into RBFOX2 isoforms is warranted.
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