Mammalian GPI-anchor modifications and the enzymes involved.

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  • Author(s): Liu YS;Liu YS; Fujita M; Fujita M
  • Source:
    Biochemical Society transactions [Biochem Soc Trans] 2020 Jun 30; Vol. 48 (3), pp. 1129-1138.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Portland Press On The Behalf Of The Biochemical Society Country of Publication: England NLM ID: 7506897 Publication Model: Print Cited Medium: Internet ISSN: 1470-8752 (Electronic) Linking ISSN: 03005127 NLM ISO Abbreviation: Biochem Soc Trans Subsets: MEDLINE
    • Publication Information:
      Original Publication: London : Portland Press On The Behalf Of The Biochemical Society
    • Subject Terms:
      Cell Membrane/*metabolism ; Endoplasmic Reticulum/*enzymology ; Glycosylphosphatidylinositols/*biosynthesis ; Golgi Apparatus/*enzymology; Animals ; Humans ; Male ; Membrane Microdomains/enzymology ; Membrane Proteins/metabolism ; Neurogenesis ; Protein Domains ; Protein Folding ; Protein Transport ; Spermatogenesis
    • Abstract:
      Glycosylphosphatidylinositol (GPI) is a glycolipid added to the C-terminus of a large variety of proteins in eukaryotes, thereby anchoring these proteins to the cell surface. More than 150 different human proteins are modified with GPI, and GPI-anchored proteins (GPI-APs) play critical roles in embryogenesis, neurogenesis, immunity, and fertilization. GPI-APs are biosynthesized in the endoplasmic reticulum (ER) and transported to the plasma membrane via the Golgi apparatus. During transport, GPI-APs undergo structural remodeling that is important for the efficient folding and sorting of GPI-APs. Asparagine-linked glycan-dependent folding and deacylation by PGAP1 work together to ensure that correctly folded GPI-APs are transported from the ER to the Golgi. Remodeling of the GPI lipid moiety is critical for the association of GPI-APs with lipid rafts. On the cell surface, certain GPI-APs are cleaved by GPI cleavage enzymes and released from the membrane, a key event in processes such as spermatogenesis and neurogenesis. In this review, we discuss the enzymes involved in GPI-AP biosynthesis and the fate of GPI-APs in mammalian cells, with a focus on the assembly, folding, degradation, and cleavage of GPI-APs.
      (© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.)
    • Accession Number:
      0 (Glycosylphosphatidylinositols)
      0 (Membrane Proteins)
    • Publication Date:
      Date Created: 20200624 Date Completed: 20210219 Latest Revision: 20210219
    • Publication Date:
      20231215
    • Accession Number:
      10.1042/BST20191142
    • Accession Number:
      32573677