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2005 Fiscal Year Final Research Report Summary

The regulation of functions and expressions of proteins by glycosylphosphatidylinositol-anchor

Research Project

Project/Area Number 16570116
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Functional biochemistry
Research InstitutionOsaka University

Principal Investigator

MAEDA Yusuke  Osaka University, Research Insitute for Microbial Diseases, Associate Professor, 微生物病研究所, 助教授 (00294124)

Co-Investigator(Kenkyū-buntansha) KINOSHITA Taroh  Osaka University, Research Institute for Microbial Diseases, Professor, 微生物病研究所, 教授 (10153165)
MURAKAMI Yoshiko  Osaka University, Research Institute for Microbial Diseases, Research Associate, 微生物病研究所, 助手 (00304048)
Project Period (FY) 2004 – 2005
KeywordsGPI-anchor / transport / remodeling / de-acylation / raft
Research Abstract

(I)Identification of inositol deacylase for GPI (PGAP1).
We identified an inositol deacylase (PGAP1) by expression cloning using deacylase-deficient mutant cells we established and reported that the defect caused the delayed transport of GPI-APs.
(II)Establishment of PGAP1 knockout mice to clarify the biological significance.
We established PGAP1 knockout mice. The majority of PGAP1 null mice was lethal in embryonic stage and showed otocephaly. The other null mice had growth retardation but normal life span. The adult males of null mice were sterile due to defective entrance to oviducts and attachment to egg cells, although the number and motility of sperm was normal.
(III)Lipid remodeling of GPI-anchor and its effects upon the correct sorting and raft association of GPI-APs
We established mutant cell line in which the surface expression of GPI-APs was decreased and identified a new gene, PGAP2, responsible for the defect by expression cloning. The detail analysis of mutants strongly indicated the defect of lipid remodeling of PI portion of GPI-APs during the transport from ER to PM. To understand the defect more in detail, we established double mutant cells whose surface expression of GPI-APs was restored by mutagenizing PGAP2-deficient cells. In double mutant cells, GPI had highly unsaturated lipid chains at sn-2 position of PI, whereas GPI in wild cells exclusively had saturated lipid chain. Moreover such GPI-APs with unsaturated lipid chains associated with rafts much weaker than wild-type cells. These results were first evidences proving that lipid remodeling of GPI takes place in mammalian cells and that lipid remodeling is critical for association of GPI-APs with rafts.

  • Research Products

    (12 results)

All 2006 2005 2004

All Journal Article (12 results)

  • [Journal Article] PGAP2 Is Essential for Correct Processing and Stable Expression of GPI-anchored Proteins.2006

    • Author(s)
      Yuko Tashima
    • Journal Title

      Mol.Biol.Cell 17

      Pages: 1410-1420

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei.2006

    • Author(s)
      Hong Y
    • Journal Title

      FEBS Lett. 580

      Pages: 603-606

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins.2006

    • Author(s)
      Tashima, Y., et al.
    • Journal Title

      Mol.Biol.Cell. 17

      Pages: 1410-1420

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei.2006

    • Author(s)
      Hong, Y., et al.
    • Journal Title

      FEBS Lett. 580

      Pages: 603-606

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component.2005

    • Author(s)
      Yoshiko Murakami
    • Journal Title

      Mol.Biol.Cell 16

      Pages: 5236-5246

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol.2005

    • Author(s)
      Kang JY
    • Journal Title

      J Biol Chem. 280

      Pages: 9489-9497

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I.2005

    • Author(s)
      Hisashi Ashida
    • Journal Title

      Mol.Biol.Cell 16

      Pages: 1439-1448

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] The Initial Enzyme for Glycosylphosphatidylinositol Biosynthesis Requires PIG-Y, a Seventh Component.2005

    • Author(s)
      Murakami, Y., et al.
    • Journal Title

      Mol Biol Cell. 16

      Pages: 5236-5246

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol.2005

    • Author(s)
      Kang, JY., et al.
    • Journal Title

      J Biol Chem. 280

      Pages: 9489-9497

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I.2005

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

      Mol Biol Cell. 16

      Pages: 1439-1448

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Inositol-deacylation of glycosylphosphatidylinositol- anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p.2004

    • Author(s)
      Satoshi Tanaka
    • Journal Title

      J.Biol.Chem. 279

      Pages: 14256-14263

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Inositol-deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p2004

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

      J Biol Chem. 279

      Pages: 14256-142

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2007-12-13  

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