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Vol. 13, Issue 5, 1694-1708, May 2002

Yeast Vps55p, a Functional Homolog of Human Obesity Receptor Gene-related Protein, Is Involved in Late Endosome to Vacuole Trafficking

Naïma Belgareh-Touzé,^* Sandrine Avaro,^* Yves Rouillé, Bernard Hoflack, and Rosine Haguenauer-Tsapis^*

 ^*Jacques Monod Institute, Centre National de la Recherche Scientifique Unité Mixte de Recherche 7592, Universities Paris VI and VII, Paris Cedex 05, France;  Pasteur Institute, Centre National de la Recherche Scientifique EP525, Lille, France 59021

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 show 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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Corresponding author. E-mail address: haguenauer{at}ijm.jussieu.fr.

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Molecular Biology of the Cell
Vol. 13, 1694-1708, May 2002
Copyright © 2002 by The American Society for Cell Biology

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