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Vol. 13, Issue 7, 2518-2532, July 2002
Molecular Membrane Biology Laboratory, RIKEN, Saitama 351-0198, Japan
The yeast open reading frame YLR080w/EMP46 encodes a
homolog of the Golgi protein Emp47p. These two proteins are 45%
identical and have a single transmembrane domain in their C-terminal
regions and a carbohydrate recognition domain signature in the
N-terminal region. The C-terminal tail of Emp46p includes a dilysine
signal. This protein is localized to Golgi membranes at steady state by subcellular fractionation and green fluorescent protein labeling. On
block of forward transport in sec12-4 cells,
redistribution of Emp46p from the Golgi to the endoplasmic reticulum is
observed. These localization features are similar to those previously
reported for Emp47p. In addition, mutagenesis of the C-terminal region identified a tyrosine-containing motif as a critical determinant of the
Golgi-localization and interaction with both COPI and COPII components.
Similar motifs are also observed in the C-terminal tail of Emp47p and
other mammalian homologs. Disruption of Emp47p displays a growth defect
at a high temperature or on Ca2+-containing medium, which
is rescued by overexpression of Emp46p, suggesting a partially
overlapping function between Emp46p and Emp47p. In addition, we found
that the disruption of both Emp46p and Emp47p show a marked defect in
the secretion of a subset of glycoproteins. Analysis of the C-terminal
mutants for Ca2+ sensitivity revealed that the forward
transport of Emp46/47p is essential for their function, whereas the
retrograde transport is not. We propose that Emp46p and Emp47p are
required for the export of specific glycoprotein cargo from the
endoplasmic reticulum.
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