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Originally published In Press as doi:10.1074/jbc.M200090200 on January 15, 2002

J. Biol. Chem., Vol. 277, Issue 12, 10547-10554, March 22, 2002
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Retention of the Yeast Sac1p Phosphatase in the Endoplasmic Reticulum Causes Distinct Changes in Cellular Phosphoinositide Levels and Stimulates Microsomal ATP Transport*

Gerlinde Konrad, Tanja Schlecker, Frank Faulhammer, and Peter MayingerDagger

From the Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany

The yeast phosphoinositide phosphatase Sac1p localizes to endoplasmic reticulum (ER) and Golgi membranes and has compartment-specific functions in these organelles. In this study we analyzed in detail the topology of Sac1p. Our data show that Sac1p is a type II transmembrane protein with a large N-terminal cytosolic domain, which is anchored in the membrane by the two potential transmembrane helices near the C terminus. Based on this topology, we created a mutation that caused retention of Sac1p in the ER and as a consequence showed specific alterations in cellular phosphoinositide levels. Our results suggest that Sac1p controls a pool of phosphatidylinositol 3-phosphate and phosphatidylinositol 4-phosphate in the ER. Retention of Sac1p in the ER also stimulates ATP transport into the ER lumen but causes the same Golgi-specific defects that are seen in a sac1 null mutant. Taken together this study provides evidence that Sac1p is an important 4-phosphatase in the ER controlling different aspects of ER-based protein processing and secretion.

* This work was supported by Grant Ma1363/5-1 from the Deutsche Forschungsgemeinschaft and the SFB 352.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 49-6221-546823; Fax.: 49-6221-545892; E-mail: mayingerp@sun0.urz.uni-heidelberg.de.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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