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Lipid trafficking

Exchange by ORDer

Nature Reviews Molecular Cell Biology volume 11, pages 86–87 (2010)Cite this article

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ORPs contain an OSBP-related domain (ORD) with a sterol-binding pocket. Some ORDs are thought to also bind phosphatidylinositol phosphates (PtdInsPs) at another surface. The authors show that ORDs purified from yeast cause aggregation of liposomes (structures made of phospholipids), suggesting that this domain can bind two membranes simultaneously. Using the representative ORP Osh4 (also known as Kes1), which consists almost entirely of an ORD, they identified a second membrane-binding surface — distal to the sterol-binding pocket — that was necessary for liposome aggregation.

“regulated lipid transfer could transmit signals between organelles”

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References

ORIGINAL RESEARCH PAPER

  1. Schultz, T. A. et al. Lipid-regulated transfer between closely apposed membranes by oxysterol-binding protein homologues. J. Cell Biol. 187, 889–903 (2009)

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FURTHER READING

  1. Holthius, J. C. M. & Levine, T. P. Lipid traffic: floppy drives and a superhighway. Nature Rev. Mol. Cell Biol. 6, 209–220 (2005)

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Authors and Affiliations

  1. Online Editor, Lipidomics Gateway ,

    Emma Leah

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  1. Emma Leah
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Leah, E. Exchange by ORDer. Nat Rev Mol Cell Biol 11, 86–87 (2010). https://doi.org/10.1038/nrm2840

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