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A more recent version of this article appeared on March 15, 2002
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M200090200v1
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Papers In Press, published online ahead of print January 15, 2002
J. Biol. Chem, 10.1074/jbc.M200090200
Submitted on January 4, 2002
Revised on January 15, 2002
Accepted on January 14, 2002

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 Mayinger

Biology, Zentrum fuer Molekulare Biologie, 69120 Heidelberg 69120

Corresponding Author: mayingerp{at}sun0.urz.uni-heidelberg.de

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 which 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.


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