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Vol. 10, Issue 4, 1043-1059, April 1999
and
*Department of Membrane Biochemistry, Max-Planck-Institute for
Biochemistry, 82152 Martinsried, Germany; and Many eukaryotic cell surface proteins are anchored in the lipid
bilayer through glycosylphosphatidylinositol (GPI).
GPI anchors are covalently attached in the endoplasmic reticulum (ER).
The modified proteins are then transported through the secretory
pathway to the cell surface. We have identified two genes in
Saccharomyces cerevisiae, LAG1 and a
novel gene termed DGT1 (for "delayed GPI-anchored protein transport"), encoding structurally related proteins
with multiple membrane-spanning domains. Both proteins are localized to
the ER, as demonstrated by immunofluorescence microscopy. Deletion of
either gene caused no detectable phenotype, whereas lag1Howard
Hughes Medical Institute and Department of Biochemistry and Biophysics,
University of California Medical School, San Francisco, California
94143-0448
dgt1 cells displayed growth defects and a significant delay
in ER-to-Golgi transport of GPI-anchored proteins, suggesting that
LAG1 and DGT1 encode functionally
redundant or overlapping proteins. The rate of GPI anchor attachment
was not affected, nor was the transport rate of several
non-GPI-anchored proteins. Consistent with a role of Lag1p and Dgt1p
in GPI-anchored protein transport, lag1 dgt1 cells
deposit abnormal, multilayered cell walls. Both proteins have
significant sequence similarity to TRAM, a mammalian membrane protein thought to be involved in protein translocation across the ER
membrane. In vivo translocation studies, however, did not detect any
defects in protein translocation in lag1 dgt1
cells, suggesting that neither yeast gene plays a role in this process. Instead, we propose that Lag1p and Dgt1p facilitate efficient ER-to-Golgi transport of GPI-anchored proteins.
Corresponding author. E-mail address:
barz{at}biochem.mpg.de.
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