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A more recent version of this article appeared on May 1, 2002
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Submitted on December 27, 2001
Accepted on February 15, 2002
1 Jacques Monod Institute, CNRS UMR7592, Universities Paris VI and VII, 2 place Jussieu, 75251 PARIS Cedex 05
2 Pasteur Institute, CNRS EP525, 1 rue Calmette BP 447, 59021 Lille Cedex
* Corresponding author. E-mail address: haguenauer{at}ijm.jussieu.fr.
The Saccharomyces cerevisiae VPS55 (YJR044c) gene encodes a small protein of 140 amino acids with four potential transmembrane domains. VPS55 belongs to a family of genes of unknown function, including the human gene encoding the Obesity Receptor Gene Related Protein (OB-RGRP). Yeast cells with a disrupted VPS55 present normal vacuolar morphology, but exhibit an abnormal secretion of the Golgi form of the soluble vacuolar carboxypeptidase Y. However, trafficking of the membrane-bound vacuolar alkaline phosphatase remains normal. The endocytosis of uracil permease, used as an endocytic marker, is normal in vps55· cells, but its degradation is delayed and this marker transiently accumulates in late endosomal compartments. We also found that Vps55p is mainly localized in the late endosomes. Collectively, these results indicate that Vps55p is involved in late endosome to vacuole trafficking. Finally, we showed that human OB-RGRP displays the same distribution as Vps55p and corrects the phenotypic defects of the vps55· strain. Therefore, the function of Vps55p has been conserved throughout evolution. This study highlights the importance of the multispanning Vps55p and OB-RGRP in membrane trafficking to the vacuole/lysosome of eukaryotic cells.
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