A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP - PubMed (original) (raw)

. 2013 Nov 7;155(4):830-43.

doi: 10.1016/j.cell.2013.09.056.

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• PMID: 24209621
• DOI: 10.1016/j.cell.2013.09.056

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A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP

Bruno Mesmin et al. Cell. 2013.

Free article

Abstract

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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Comment in

• A twoferase for lipid transfer at ER-golgi contact sites.
  Levine TP. Levine TP. Dev Cell. 2013 Nov 25;27(4):369-70. doi: 10.1016/j.devcel.2013.11.009. Dev Cell. 2013. PMID: 24286822
• The lipid trade.
  Prinz WA. Prinz WA. Nat Rev Mol Cell Biol. 2014 Feb;15(2):79. doi: 10.1038/nrm3740. Epub 2014 Jan 17. Nat Rev Mol Cell Biol. 2014. PMID: 24434885 Free PMC article. No abstract available.

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