Journal
CELL
Volume 155, Issue 4, Pages 830-843Publisher
CELL PRESS
DOI: 10.1016/j.cell.2013.09.056
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Funding
- CNRS
- Agence Nationale de la Recherche [ANR-10-JCJC-1503-01, ANR-11-LABX-0028-01]
- ERC [268888]
- European Research Council (ERC) [268888] Funding Source: European Research Council (ERC)
- Agence Nationale de la Recherche (ANR) [ANR-10-JCJC-1503] Funding Source: Agence Nationale de la Recherche (ANR)
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Several proteins at endoplasmic reticulum (ER)-Golgi membrane contact sites contain a PH domain that interacts with the Golgi phosphoinositide PI(4) P, a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain. This architecture suggests the ability to both tether organelles and transport lipids between them. We show that in oxysterol binding protein (OSBP) these two activities are coupled by a four-step cycle. Membrane tethering by the PH domain and the FFAT motif enables sterol transfer by the lipid transfer domain (ORD), followed by back transfer of PI(4) P by the ORD. Finally, PI(4) P is hydrolyzed in cis by the ER protein Sac1. The energy provided by PI(4) P hydrolysis drives sterol transfer and allows negative feedback when PI(4) P becomes limiting. Other lipid transfer proteins are tethered by the same mechanism. Thus, OSBP-mediated back transfer of PI(4) P might coordinate the transfer of other lipid species at the ER-Golgi interface.
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