Nonvesicular Lipid Transfer from the Endoplasmic Reticulum

Lev, Sima

doi:10.1101/cshperspect.a013300

Cited by 99 publications

(84 citation statements)

References 117 publications

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“…Coat protein complex II (COPII)-coated vesicles mediate transport of both lipids and proteins to the Golgi compartment (Gillon et al, 2012;Perry and Ridgway, 2005). In addition to COPII-dependent vesicular transport, non-vesicular mechanisms are used for delivery of lipids from the ER to other compartments (Lev, 2012;Perry and Ridgway, 2005;Prinz, 2010). The bestcharacterized example of a lipid that is delivered to the Golgi by non-vesicular mechanisms is ceramide (Perry and Ridgway, 2005;Prinz, 2010).…”

Section: Introductionmentioning

confidence: 99%

Osh proteins regulate COPII-mediated vesicular transport of ceramide from the endoplasmic reticulum in budding yeast

Kajiwara

Ikeda

Aguilera-Romero

et al. 2013

Journal of Cell Science

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Lipids synthesized at the endoplasmic reticulum (ER) are delivered to the Golgi by vesicular and non-vesicular pathways. ER-to-Golgi transport is crucial for maintaining the different membrane lipid composition and identities of organelles. Despite their importance, mechanisms regulating transport remain elusive. Here we report that in yeast coat protein complex II (COPII) vesicle-mediated transport of ceramide from the ER to the Golgi requires oxysterol-binding protein homologs, Osh proteins, which have been implicated in lipid homeostasis. Because Osh proteins are not required to transport proteins to the Golgi, these results indicate a specific requirement for the Osh proteins in the transport of ceramide. In addition, we provide evidence that Osh proteins play a negative role in COPII vesicle biogenesis. Together, our data suggest that ceramide transport and sphingolipid levels between the ER and Golgi are maintained by two distinct functions of Osh proteins, which negatively regulate COPII vesicle formation and positively control a later stage, presumably fusion of ceramide-enriched vesicles with Golgi compartments.

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Section: Introductionmentioning

confidence: 99%

Osh proteins regulate COPII-mediated vesicular transport of ceramide from the endoplasmic reticulum in budding yeast

Kajiwara

Ikeda

Aguilera-Romero

et al. 2013

Journal of Cell Science

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“…called spontaneous lipid transfer (SLT) (Brown 1992;Lev 2012). Transfer rates between unilamellar vesicles suggest that transport of e.g.…”

Section: Introductionmentioning

confidence: 99%

“…First, LTPs, carrying a lipophilic binding pocket that encases the lipid during diffusion, catalyze the reaction (Neumann and van Meer 2008;Clark 2012;Lev 2012). When the distance between donor and acceptor membranes is short, e.g.…”

Section: Introductionmentioning

confidence: 99%

No Evidence for Spontaneous Lipid Transfer at ER–PM Membrane Contact Sites

et al. 2015

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Non-vesicular lipid transport steps play a crucial role in lipid trafficking and potentially include spontaneous exchange. Since membrane contact facilitates this lipid transfer, it is most likely to occur at membrane contact sites (MCS). However, to date it is unknown whether closely attached biological membranes exchange lipids spontaneously. We have set up a system for studying the exchange of lipids at MCS formed between the endoplasmic reticulum (ER) and the plasma membrane. Contact sites were stably anchored and the lipids cholesterol and phosphatidylcholine (PC) were not capable of transferring spontaneously into the opposed bilayer. We conclude that physical contact between two associated biological membranes is not sufficient for transfer of the lipids PC and cholesterol.

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“…In addition, the nonextractable membrane-spanning reporter molecules may also be helpful in the study of the selectivity and requirements of other LTPs. These LTPs are ubiquitous in the cytoplasm of eukaryotic cells and are involved, for instance, in intermembrane transfer of oxysterol and phospholipids (76)(77)(78)(79), as well as Cer derivatives and glycolipids ( 1,64,80,81 ). Furthermore, these FRET assays allow us to study in real time, without the need to separate vesicles, and in more detail the activities of activator proteins and their variant forms.…”

Section: Conclusion and Prospectsmentioning

confidence: 99%