Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae.

Biochim Biophys Acta

Department of Medicine, Division of Biochemistry, Chemin du Musée 5, CH-1700 Fribourg, Switzerland.

Published: March 2007

AI Article Synopsis

  • - Saccharomyces cerevisiae, like other eukaryotes, uses a GPI anchoring system to attach proteins to membranes, with many of these proteins subsequently integrated into the cell wall via covalent bonds to glucans.
  • - The GPI biosynthetic pathway is essential for yeast growth and survival, involving 12 steps and 23 genes, of which 19 are critical for the process.
  • - With around 60 predicted GPI proteins, some function in biosynthesis and cell wall maintenance, while others provide structure or support cell adhesion, making S. cerevisiae an excellent model for studying GPI processes and fungal cell wall formation.

Article Abstract

Like most other eukaryotes, Saccharomyces cerevisiae harbors a GPI anchoring machinery and uses it to attach proteins to membranes. While a few GPI proteins reside permanently at the plasma membrane, a majority of them gets further processed and is integrated into the cell wall by a covalent attachment to cell wall glucans. The GPI biosynthetic pathway is necessary for growth and survival of yeast cells. The GPI lipids are synthesized in the ER and added onto proteins by a pathway comprising 12 steps, carried out by 23 gene products, 19 of which are essential. Some of the estimated 60 GPI proteins predicted from the genome sequence serve enzymatic functions required for the biosynthesis and the continuous shape adaptations of the cell wall, others seem to be structural elements of the cell wall and yet others mediate cell adhesion. Because of its genetic tractability S. cerevisiae is an attractive model organism not only for studying GPI biosynthesis in general, but equally for investigating the intracellular transport of GPI proteins and the peculiar role of GPI anchoring in the elaboration of fungal cell walls.

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http://dx.doi.org/10.1016/j.bbalip.2006.05.015DOI Listing

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