Please use this identifier to cite or link to this item: https://doi.org/10.1126/science.aab1370
Title: PI4P/phosphatidylserine countertransport at ORP5-and ORP8-mediated ER-plasma membrane contacts
Authors: Chung, Jeeyun
Torta, Federico
Masai, Kaori
Lucast, Louise
Czapla, Heather
Tanner, Lukas B
Narayanaswamy, Pradeep
Wenk, Markus R 
Nakatsu, Fubito
De Camilli, Pietro
Keywords: Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
OXYSTEROL-BINDING-PROTEINS
PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE LEVELS
PHOSPHATIDYLSERINE
SITES
4-PHOSPHATE
METABOLISM
TRANSPORT
REVEALS
STEROL
PIPELINES
Issue Date:  24
Publisher: AMER ASSOC ADVANCEMENT SCIENCE
Citation: Chung, Jeeyun, Torta, Federico, Masai, Kaori, Lucast, Louise, Czapla, Heather, Tanner, Lukas B, Narayanaswamy, Pradeep, Wenk, Markus R, Nakatsu, Fubito, De Camilli, Pietro (24). PI4P/phosphatidylserine countertransport at ORP5-and ORP8-mediated ER-plasma membrane contacts. SCIENCE 349 (6246) : 428-432. ScholarBank@NUS Repository. https://doi.org/10.1126/science.aab1370
Abstract: Copyright 2015 by the American Association for the Advancement of Science. Lipid transfer between cell membrane bilayers at contacts between the endoplasmic reticulum (ER) and other membranes help to maintain membrane lipid homeostasis. We found that two similar ER integral membrane proteins, oxysterol-binding protein (OSBP)-related protein 5 (ORP5) and ORP8, tethered the ER to the plasma membrane (PM) via the interaction of their pleckstrin homology domains with phosphatidylinositol 4-phosphate (PI4P) in this membrane. Their OSBP - related domains (ORDs) harbored either PI4P or phosphatidylserine (PS) and exchanged these lipids between bilayers. Gain- and loss-of-function experiments showed that ORP5 and ORP8 could mediate PI4P/PS countertransport between the ER and the PM, thus delivering PI4P to the ER-localized PI4P phosphatase Sac1 for degradation and PS from the ER to the PM. This exchange helps to control plasma membrane PI4P levels and selectively enrich PS in the PM.
Source Title: SCIENCE
URI: https://scholarbank.nus.edu.sg/handle/10635/173255
ISSN: 00368075
10959203
DOI: 10.1126/science.aab1370
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