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Published 18 January 2005. doi:10.1083/jcb.200407118
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 2, 185-191
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Cell growth–dependent coordination of lipid signaling and glycosylation is mediated by interactions between Sac1p and Dpm1p



Frank Faulhammer1, Gerlinde Konrad2, Ben Brankatschk1, Sabina Tahirovic2, Andreas Knödler1, and Peter Mayinger1

1 Division of Nephrology and Hypertension, Oregon Health & Science University, Portland, OR 97239
2 Zentrum für Molekulare Biologie der Universität Heidelberg, D-69120 Heidelberg, Germany

Correspondence to Peter Mayinger: mayinger{at}ohsu.edu


Abstract

The integral membrane lipid phosphatase Sac1p regulates local pools of phosphatidylinositol-4-phosphate (PtdIns(4)P) at endoplasmic reticulum (ER) and Golgi membranes. PtdIns(4)P is important for Golgi trafficking, yet the significance of PtdIns(4)P for ER function is unknown. It also remains unknown how localization of Sac1p to distinct organellar membranes is mediated. Here, we show that a COOH-terminal region in yeast Sac1p is crucial for ER targeting by directly interacting with dolicholphosphate mannose synthase Dpm1p. The interaction with Dpm1p persists during exponential cell division but is rapidly abolished when cell growth slows because of nutrient limitation, causing translocation of Sac1p to Golgi membranes. Cell growth–dependent shuttling of Sac1p between the ER and the Golgi is important for reciprocal control of PtdIns(4)P levels at these organelles. The fraction of Sac1p resident at the ER is also required for efficient dolichol oligosaccharide biosynthesis. Thus, the lipid phosphatase Sac1p may be a key regulator, coordinating the secretory capacity of ER and Golgi membranes in response to growth conditions.

Abbreviations used in this paper: BMH, 1,6-bis-maleimidohexane; CPY, carboxypeptidase Y; Dol-P-Man, dolichol phosphate mannose; PtdIns, phosphatidylinositol.


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