Cell growth-dependent coordination of lipid signaling and glycosylation is mediated by interactions between Sac1p and Dpm1p

被引:56
作者
Faulhammer, F
Konrad, G
Brankatschk, B
Tabirovic, S
Knödler, A
Mayinger, P [1 ]
机构
[1] Oregon Hlth Sci Univ, Div Nephrol & Hypertens, Portland, OR 97239 USA
[2] Univ Heidelberg, Zentrum Mol Biol, D-69120 Heidelberg, Germany
关键词
D O I
10.1083/jcb.200407118
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
T he 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 secretary capacity of ER and Golgi membranes in response to growth conditions.
引用
收藏
页码:185 / 191
页数:7
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