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Stefan CJ, et al.  (2011) Osh Proteins Regulate Phosphoinositide Metabolism at ER-Plasma Membrane Contact Sites. Cell 144(3):389-401

Abstract: Sac1 phosphoinositide (PI) phosphatases are essential regulators of PI-signaling networks. Yeast Sac1, an integral endoplasmic reticulum (ER) membrane protein, controls PI4P levels at the ER, Golgi, and plasma membrane (PM). Whether Sac1 can act in trans and turn over PI4P at the Golgi and PM from the ER remains a paradox. We find that Sac1-mediated PI4P metabolism requires the oxysterol-binding homology (Osh) proteins. The PH domain-containing family member, Osh3, localizes to PM/ER membrane contact sites dependent upon PM PI4P levels. We reconstitute Osh protein-stimulated Sac1 PI phosphatase activity in vitro. We also show that the ER membrane VAP proteins, Scs2/Scs22, control PM PI4P levels and Sac1 activity in vitro. We propose that Osh3 functions at ER/PM contact sites as both a sensor of PM PI4P and an activator of the ER Sac1 phosphatase. Our findings further suggest that the conserved Osh proteins control PI metabolism at additional membrane contact sites.CI - Copyright (c) 2011 Elsevier Inc. All rights reserved.

Status: Published Type: Journal Article PubMed ID: 21295699

Topics addressed in this paper

Number of different genes curated to this paper: 12

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Topics Genes linked to topics (#1 - 10 )
HES1 KES1 OSH2 OSH3 OSH6 OSH7 PIK1 SAC1 SCS2 SCS22
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Protein-protein Interactions blue ball blue ball
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Topics Genes linked to topics (#11 - 12 )
STT4 SWH1
Additional Literature blue ball
Cellular Location blue ball
Function/Process blue ball
Mutants/Phenotypes blue ball
Primary Literature blue ball
Regulatory Role blue ball
Strains/Constructs blue ball

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