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Review
. 2007 Feb;6(2):119-33.
doi: 10.1128/EC.00297-06. Epub 2006 Dec 22.

Comprehensive analysis of glycosylphosphatidylinositol-anchored proteins in Candida albicans

Affiliations
Review

Comprehensive analysis of glycosylphosphatidylinositol-anchored proteins in Candida albicans

Mathias L Richard et al. Eukaryot Cell. 2007 Feb.
No abstract available

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Figures

FIG. 1.
FIG. 1.
GPI anchor structure. The core structure found in any eukaryotic cell is represented in black. The additional gray groups illustrate the side chains added to the GPI anchor in S. cerevisiae (side chains are specific to each organism). Gpi7 is a protein involved in the addition of the ethanolamine phosphate side chain to the second mannose group in S. cerevisiae and C. albicans. EtN, ethanolamine; Ins, inositol; P, phosphore.
FIG. 2.
FIG. 2.
Function repartition within the group of GPI-anchored proteins (Table 1).
FIG. 3.
FIG. 3.
Phylogenetic tree of the HYR/IFF gene family. The tree shows the relationships among Hyr1 and Iff proteins in C. albicans and C. dubliniensis (Cdub). This tree is based on protein sequence alignments of the first 350 amino acid residues after gap removal. For bootstrap analyses, we constructed this tree by the neighbor-joining method using ClustalX. Bootstrap values based on 1,000 replications are shown next to the nodes. An Iff homologue from C. glabrata was used as the out-group.
FIG. 4.
FIG. 4.
The different steps of the synthesis and transport of a GPI-anchored protein in yeasts or fungi. The first steps of GPI anchor biosynthesis occur in the ER or at its surface: synthesis of the GPI core structure and translation through the ER membrane of the future GpiP. The subsequent attachment of the protein onto the GPI anchor takes place in the ER lumen. Then the GpiPs follow the secretory pathway to be presented at the cell surface. The particularity of some fungi is an additional step in which the GPI anchor is cleaved after the glucosamine and the protein with the remnant part of the anchor is directed to the cell wall and covalently linked to β-1,6-glucan.

References

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