Tip110 interacts with YB-1 and regulates each other's function

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10 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article number14
JournalBMC Molecular Biology
Volume14
DOIs
StatePublished - 4 Jul 2013

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HIV Long Terminal Repeat
Proteins
Y-Box-Binding Protein 1
RNA Precursors
Alternative Splicing
Reporter Genes
Transcriptional Activation
Exons
Mass Spectrometry
Neoplasms

Keywords

  • Alternative Splicing
  • CD44
  • HIV-1 Tat
  • Tip110
  • Transcription
  • YB-1

Cite this

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title = "Tip110 interacts with YB-1 and regulates each other's function",
abstract = "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.",
keywords = "Alternative Splicing, CD44, HIV-1 Tat, Tip110, Transcription, YB-1",
author = "Timani, {Khalid A.} and Ying Liu and He, {Johnny Jianglin}",
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doi = "10.1186/1471-2199-14-14",
language = "English",
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Tip110 interacts with YB-1 and regulates each other's function. / Timani, Khalid A.; Liu, Ying; He, Johnny Jianglin.

In: BMC Molecular Biology, Vol. 14, 14, 04.07.2013.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

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AU - Timani, Khalid A.

AU - Liu, Ying

AU - He, Johnny Jianglin

PY - 2013/7/4

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N2 - 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.

AB - 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.

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