GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics

Biochim Biophys Acta. 2012 Aug;1821(8):1050-8. doi: 10.1016/j.bbalip.2012.01.004. Epub 2012 Jan 11.

Abstract

Glycosylphosphatidylinositol (GPI) anchoring of proteins is a conserved post-translational modification in eukaryotes. GPI is synthesized and transferred to proteins in the endoplasmic reticulum. GPI-anchored proteins are then transported from the endoplasmic reticulum to the plasma membrane through the Golgi apparatus. GPI-anchor functions as a sorting signal for transport of GPI-anchored proteins in the secretory and endocytic pathways. After GPI attachment to proteins, the structure of the GPI-anchor is remodeled, which regulates the trafficking and localization of GPI-anchored proteins. Recently, genes required for GPI remodeling were identified in yeast and mammalian cells. Here, we describe the structural remodeling and function of GPI-anchors, and discuss how GPI-anchors regulate protein sorting, trafficking, and dynamics. This article is part of a Special Issue entitled Lipids and Vesicular Transport.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Ceramides / metabolism
  • Endoplasmic Reticulum / metabolism*
  • GPI-Linked Proteins / genetics
  • GPI-Linked Proteins / metabolism*
  • Glycosylphosphatidylinositols / metabolism*
  • Golgi Apparatus / metabolism*
  • Humans
  • Membrane Microdomains / metabolism
  • Protein Processing, Post-Translational
  • Protein Transport
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Species Specificity

Substances

  • Ceramides
  • GPI-Linked Proteins
  • Glycosylphosphatidylinositols