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A more recent version of this article appeared on July 1, 2004
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Submitted on November 20, 2003
Revised on April 5, 2004
Accepted on April 8, 2004
1 Division of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Medicine, N15 W7, Kita-ku, Sapporo, 060-0815, Japan
2 Division of Molecular Biology and Information, Institute for Chemical Science, Kyoto University, Gokasho, Uji, Kyoto, 611-0011, Japan
* Corresponding author. E-mail address: k-tanaka{at}igm.hokudai.ac.jp.
Cdc50p, a transmembrane protein localized to the late endosome, is required for polarized cell growth in yeast. Genetic studies suggest that CDC50 performs a function similar to DRS2, which encodes a P-type ATPase of the aminophospholipid translocase (APT) subfamily. At low temperatures, drs2
mutant cells exhibited depolarization of cortical actin patches and mislocalization of polarity regulators, such as Bni1p and Gic1p, in a manner similar to the cdc50 mutant. Both Cdc50p and Drs2p were localized to the trans-Golgi network (TGN) and late endosome. Cdc50p was coimmunoprecipitated with Drs2p from membrane protein extracts. In cdc50 mutant cells, Drs2p resided on the endoplasmic reticulum (ER), while Cdc50p was found on the ER membrane in drs2 cells, suggesting that the association on the ER membrane is required for transport of the Cdc50p-Drs2p complex to the TGN. Lem3/Ros3p, a homolog of Cdc50p, was coimmunoprecipitated with another APT, Dnf1p; Lem3p was required for exit of Dnf1p out of the ER. Both Cdc50p-Drs2p and Lem3p-Dnf1p were confined to the plasma membrane upon blockade of endocytosis, suggesting that these proteins cycle between the exocytic and endocytic pathways, likely performing redundant functions. Thus, phospholipid asymmetry plays an important role in the establishment of cell polarity; the Cdc50p/Lem3p family likely constitute potential subunits specific to unique P-type ATPases of the APT subfamily.
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