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J Biol Chem, Vol. 274, Issue 21, 15251-15261, May 21, 1999
From the Institute of Biochemistry, University of Fribourg, Chemin
du Musée 5, CH-1700 Fribourg, Switzerland
Gpi7 was isolated by screening for
mutants defective in the surface expression of
glycosylphosphatidylinositol (GPI) proteins. Gpi7 mutants
are deficient in YJL062w, herein named GPI7. GPI7 is not
essential, but its deletion renders cells hypersensitive to Calcofluor
White, indicating cell wall fragility. Several aspects of GPI
biosynthesis are disturbed in 
gpi7. The extent of anchor remodeling, i.e. replacement of the primary lipid moiety of
GPI anchors by ceramide, is significantly reduced, and the transport of
GPI proteins to the Golgi is delayed. Gpi7p is a highly glycosylated integral membrane protein with 9-11 predicted transmembrane domains in
the C-terminal part and a large, hydrophilic N-terminal ectodomain. The
bulk of Gpi7p is located at the plasma membrane, but a small amount is
found in the endoplasmic reticulum. GPI7 has homologues in
Saccharomyces cerevisiae, Caenorhabditis
elegans, and man, but the precise biochemical function of this
protein family is unknown. Based on the analysis of M4, an abnormal GPI
lipid accumulating in gpi7, we propose that Gpi7p adds a
side chain onto the GPI core structure. Indeed, when compared with
complete GPI lipids, M4 lacks a previously unrecognized
phosphodiester-linked side chain, possibly an ethanolamine phosphate.
Gpi7p contains significant homology with phosphodiesterases suggesting
that Gpi7p itself is the transferase adding a side chain to the
1,6-linked mannose of the GPI core structure.
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