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DNA Repair System and Transcription Regulatory Mechanisms in Pancreatic Acinar Cells.

Research Project

Project/Area Number 17590694
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Gastroenterology
Research InstitutionInstitute for Developmental Research, Aichi Hunan Service Center

Principal Investigator

INAGUMA Yutaka  Institute for Developmental Research, Department of Molecular Neurobiology, 神経制御学部, 主任研究員 (10250250)

Co-Investigator(Kenkyū-buntansha) WATANABE Kimi  Institute for Developmental Research, Research Management and Support Service, 研究企画調整科, 研究助手 (50393145)
Project Period (FY) 2005 – 2006
Project Status Completed (Fiscal Year 2006)
Budget Amount *help
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2006: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 2005: ¥2,300,000 (Direct Cost: ¥2,300,000)
KeywordsSUMO / pancreas / acinar cell / ubiquitin-like protein / TTRAP / UBC9 / FOXP2 / SMAD4
Research Abstract

We found that both SUMO-1 and SUMO-2 were present at high levels in pancreatic acinar cells and investigated its significance. TTRAP was isolated as a partner to interact with SUMO-2 when a yeast two-hybrid screening was performed. TTRAP has features as a phosphodiesterase and showed a weak AP-endonuclease-like activity. We further investigated that FOXP2 interacted with TTRAP and UBC9, a specific conjugating enzyme of SUMO. FOXP2 is a transcription factor and is expressed in the various tissues. We confirmed that FOXP2 was present in the pancreas by the Western blot analysis. In the present study, to determine the target site for sumoylation of FOXP2, eukaryotic sumoylation in Escherichia coli was performed. Three sites (K74, K274, and K673) were predicted as candidates to be sumoylated in silico. As a result, when lysine at 673 was substituted by arginine, the sumoylation of FOXP2 was lost. This indicated that K673 was the target residue to be sumoylated. Furthermore, we investigated transcriptional activities of wild type and K673R by using a reporter assay. The reporter gene was driven under the thymidine kinase promotor, and the FOXP2-binding sequence from CC10 gene was inserted into the reporter vector. The repression by K673R was stronger than the one by wild type suggesting that the sumoylation of FOXP2 affected the DNA-binding activity.

Report

(3 results)
  • 2006 Annual Research Report   Final Research Report Summary
  • 2005 Annual Research Report
  • Research Products

    (6 results)

All 2006 2005

All Journal Article (6 results)

  • [Journal Article] Fates of Cdh23/CDH23 with mutations affecting the cytoplasmic region.2006

    • Author(s)
      Yonezawa S, et al.
    • Journal Title

      Hum Mutat 27

      Pages: 88-97

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2006 Final Research Report Summary
  • [Journal Article] Fates of Cdh23/CDH23 with mutations affecting the cytoplasmic region.2006

    • Author(s)
      Yonezawa S, Yoshizaki N, Kageyama T, Takahashi T, Sano M, Tokita Y, Masaki S, Inaquma Y, Hanai A, Sakurai N, Yucky A, Kuaka M, Moriyama A, Nakayama A
    • Journal Title

      Hum Mutat. 27(1)

      Pages: 88-97

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2006 Final Research Report Summary
  • [Journal Article] Fates of Cdh23/CDH23 with mutations affecting the cytoplasmic region.2006

    • Author(s)
      Yonezawa S, et al.
    • Journal Title

      Hum Mutat. 27

      Pages: 88-97

    • Related Report
      2005 Annual Research Report
  • [Journal Article] Endoplasmic reticulum stress induces the phosphorylation of small heat shock protein, Hsp27.2005

    • Author(s)
      Ito H, et al.
    • Journal Title

      J Cell Biochem 95

      Pages: 932-941

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2006 Final Research Report Summary
  • [Journal Article] Endoplasmic reticulum stress induces the phosphorylation of small heat shock protein, Hsp27.2005

    • Author(s)
      Ito H, Iwamoto I, Inaquma Y, Takizawa T, Nagata K, Asano T, Kato K
    • Journal Title

      J Cell Biochem. 95(5)

      Pages: 932-941

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2006 Final Research Report Summary
  • [Journal Article] Endoplasmic reticulum stress induces the phosphorylation of small heat shock protein, Hsp27.2005

    • Author(s)
      Ito H, et al.
    • Journal Title

      J Cell Biochem. 95

      Pages: 932-941

    • Related Report
      2005 Annual Research Report

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Published: 2005-04-01   Modified: 2016-04-21  

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