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Extraction and Quantification of Soluble, Radiolabeled Inositol Polyphosphates from Different Plant Species using SAX-HPLC
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Biosynthesis and deficiencies of glycosylphosphatidylinositol

Taroh Kinoshita1

  • 1WPI Immunology Frontier Research Center and Research Institute for Microbial Diseases, Osaka University.

Proceedings of the Japan Academy. Series B, Physical and Biological Sciences
|April 15, 2014
PubMed

Insights

Glycosylphosphatidylinositol (GPI) anchors proteins to the cell membrane. Mutations in PIG and PGAP genes cause GPI anchor deficiencies, impacting protein attachment and cell function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Over 150 human proteins utilize glycosylphosphatidylinositol (GPI) anchors for plasma membrane localization.
  • GPI anchors are synthesized and attached to proteins in the endoplasmic reticulum via a post-translational modification mediated by GPI transamidase.

Purpose of the Study:

  • To review the characteristics of the 26 Phosphatidyl Inositol Glycan (PIG) and Post GPI Attachment to Proteins (PGAP) genes.
  • To summarize GPI anchor deficiencies resulting from mutations in PIG and PGAP genes.

Main Methods:

  • Literature review of PIG and PGAP genes involved in GPI biosynthesis, protein attachment, and remodeling.
  • Characterization of GPI anchor deficiencies caused by somatic and germline mutations.

Main Results:

  • Twenty-two PIG genes are essential for GPI biosynthesis and protein attachment.
  • Four PGAP genes are involved in the structural remodeling of GPI anchors.
  • Mutations in PIG and PGAP genes lead to various GPI anchor deficiencies.

Conclusions:

  • The PIG and PGAP gene families play critical roles in the proper functioning of GPI-anchored proteins.
  • Understanding these genes and associated deficiencies is crucial for comprehending cellular processes and potential disease mechanisms.

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