期刊论文详细信息
BMC Molecular Biology
Tip110 interacts with YB-1 and regulates each other’s function
Johnny J He1  Ying Liu1  Khalid Amine Timani1 
[1] University of North Texas Health Science Center, 3500 Camp Bowie Blvd., Fort Worth, TX 76107, USA
关键词: Transcription;    CD44;    Alternative Splicing;    YB-1;    Tip110;    HIV-1 Tat;   
Others  :  1090922
DOI  :  10.1186/1471-2199-14-14
 received in 2013-03-14, accepted in 2013-07-02,  发布年份 2013
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【 摘 要 】

Background

Tip110 plays important roles in tumor immunobiology, pre-mRNA splicing, expression regulation of viral and host genes, and possibly protein turnover. It is clear that our understanding of Tip110 biological function remains incomplete.

Results

Herein, we employed an immunoaffinity-based enrichment approach combined with protein mass spectrometry and attempted to identify Tip110-interacting cellular proteins. A total of 13 major proteins were identified to be complexed with Tip110. Among them was Y-box binding protein 1 (YB-1). The interaction of Tip110 with YB-1 was further dissected and confirmed to be specific and involve the N-terminal of both Tip110 and YB-1 proteins. A HIV-1 LTR promoter-driven reporter gene assay and a CD44 minigene in vivo splicing assay were chosen to evaluate the functional relevance of the Tip110/YB-1 interaction. We showed that YB-1 potentiates the Tip110/Tat-mediated transactivation of the HIV-1 LTR promoter while Tip110 promotes the inclusion of the exon 5 in CD44 minigene alternative splicing.

Conclusions

Tip110 and YB-1 interact to form a complex and mutually regulate each other’s biological functions.

【 授权许可】

   
2013 Timani et al.; licensee BioMed Central Ltd.

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