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A more recent version of this article appeared on July 1, 2002
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Submitted on January 16, 2002
Revised on February 28, 2002
Accepted on April 5, 2002
1 Molecular Membrane Biology Laboratory, RIKEN, Saitama 351-0198, Japan
* Corresponding author. E-mail address: kensato{at}postman.riken.go.jp.
The yeast ORF YLR080w/EMP46 encodes a homologue 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 GFP labeling. Upon block of forward transport in sec12-4 cells, redistribution of Emp46p from the Golgi to the ER 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 homologues.
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 ER.
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