ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets

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Standard

ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets. / Du, Ximing; Zhou, Linkang; Aw, Yvette Celine; Mak, Hoi Yin; Xu, Yanqing; Rae, James; Wang, Wenmin; Zadoorian, Armella; Hancock, Sarah E.; Osborne, Brenna; Chen, Xiang; Wu, Jia-Wei; Turner, Nigel; Parton, Robert G.; Li, Peng; Yang, Hongyuan.

I: Journal of Cell Biology, 2020.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Du, X, Zhou, L, Aw, YC, Mak, HY, Xu, Y, Rae, J, Wang, W, Zadoorian, A, Hancock, SE, Osborne, B, Chen, X, Wu, J-W, Turner, N, Parton, RG, Li, P & Yang, H 2020, 'ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets', Journal of Cell Biology. https://doi.org/10.1083/jcb.201905162

APA

Du, X., Zhou, L., Aw, Y. C., Mak, H. Y., Xu, Y., Rae, J., Wang, W., Zadoorian, A., Hancock, S. E., Osborne, B., Chen, X., Wu, J-W., Turner, N., Parton, R. G., Li, P., & Yang, H. (2020). ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets. Journal of Cell Biology, [e201905162]. https://doi.org/10.1083/jcb.201905162

Vancouver

Du X, Zhou L, Aw YC, Mak HY, Xu Y, Rae J o.a. ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets. Journal of Cell Biology. 2020. e201905162. https://doi.org/10.1083/jcb.201905162

Author

Du, Ximing ; Zhou, Linkang ; Aw, Yvette Celine ; Mak, Hoi Yin ; Xu, Yanqing ; Rae, James ; Wang, Wenmin ; Zadoorian, Armella ; Hancock, Sarah E. ; Osborne, Brenna ; Chen, Xiang ; Wu, Jia-Wei ; Turner, Nigel ; Parton, Robert G. ; Li, Peng ; Yang, Hongyuan. / ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets. I: Journal of Cell Biology. 2020.

Bibtex

@article{f3dad5ea001f4b729537e4a8a1f46dc4,
title = "ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets",
abstract = "Lipid droplets (LDs) are evolutionarily conserved organelles that play important roles in cellular metabolism. Each LD is enclosed by a monolayer of phospholipids, distinct from bilayer membranes. During LD biogenesis and growth, this monolayer of lipids expands by acquiring phospholipids from the endoplasmic reticulum (ER) through nonvesicular mechanisms. Here, in a mini-screen, we find that ORP5, an integral membrane protein of the ER, can localize to ER–LD contact sites upon oleate loading. ORP5 interacts with LDs through its ligand-binding domain, and ORP5 deficiency enhances neutral lipid synthesis and increases the size of LDs. Importantly, there is significantly more phosphatidylinositol-4-phosphate (PI(4)P) and less phosphatidylserine (PS) on LDs in ORP5-deficient cells than in normal cells. The increased presence of PI(4)P on LDs in ORP5-deficient cells requires phosphatidylinositol 4-kinase 2-α. Our results thus demonstrate the existence of PI(4)P on LDs and suggest that LD-associated PI(4)P may be primarily used by ORP5 to deliver PS to LDs.",
author = "Ximing Du and Linkang Zhou and Aw, {Yvette Celine} and Mak, {Hoi Yin} and Yanqing Xu and James Rae and Wenmin Wang and Armella Zadoorian and Hancock, {Sarah E.} and Brenna Osborne and Xiang Chen and Jia-Wei Wu and Nigel Turner and Parton, {Robert G.} and Peng Li and Hongyuan Yang",
year = "2020",
doi = "10.1083/jcb.201905162",
language = "English",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",

}

RIS

TY - JOUR

T1 - ORP5 localizes to ER–lipid droplet contacts and regulates the level of PI(4)P on lipid droplets

AU - Du, Ximing

AU - Zhou, Linkang

AU - Aw, Yvette Celine

AU - Mak, Hoi Yin

AU - Xu, Yanqing

AU - Rae, James

AU - Wang, Wenmin

AU - Zadoorian, Armella

AU - Hancock, Sarah E.

AU - Osborne, Brenna

AU - Chen, Xiang

AU - Wu, Jia-Wei

AU - Turner, Nigel

AU - Parton, Robert G.

AU - Li, Peng

AU - Yang, Hongyuan

PY - 2020

Y1 - 2020

N2 - Lipid droplets (LDs) are evolutionarily conserved organelles that play important roles in cellular metabolism. Each LD is enclosed by a monolayer of phospholipids, distinct from bilayer membranes. During LD biogenesis and growth, this monolayer of lipids expands by acquiring phospholipids from the endoplasmic reticulum (ER) through nonvesicular mechanisms. Here, in a mini-screen, we find that ORP5, an integral membrane protein of the ER, can localize to ER–LD contact sites upon oleate loading. ORP5 interacts with LDs through its ligand-binding domain, and ORP5 deficiency enhances neutral lipid synthesis and increases the size of LDs. Importantly, there is significantly more phosphatidylinositol-4-phosphate (PI(4)P) and less phosphatidylserine (PS) on LDs in ORP5-deficient cells than in normal cells. The increased presence of PI(4)P on LDs in ORP5-deficient cells requires phosphatidylinositol 4-kinase 2-α. Our results thus demonstrate the existence of PI(4)P on LDs and suggest that LD-associated PI(4)P may be primarily used by ORP5 to deliver PS to LDs.

AB - Lipid droplets (LDs) are evolutionarily conserved organelles that play important roles in cellular metabolism. Each LD is enclosed by a monolayer of phospholipids, distinct from bilayer membranes. During LD biogenesis and growth, this monolayer of lipids expands by acquiring phospholipids from the endoplasmic reticulum (ER) through nonvesicular mechanisms. Here, in a mini-screen, we find that ORP5, an integral membrane protein of the ER, can localize to ER–LD contact sites upon oleate loading. ORP5 interacts with LDs through its ligand-binding domain, and ORP5 deficiency enhances neutral lipid synthesis and increases the size of LDs. Importantly, there is significantly more phosphatidylinositol-4-phosphate (PI(4)P) and less phosphatidylserine (PS) on LDs in ORP5-deficient cells than in normal cells. The increased presence of PI(4)P on LDs in ORP5-deficient cells requires phosphatidylinositol 4-kinase 2-α. Our results thus demonstrate the existence of PI(4)P on LDs and suggest that LD-associated PI(4)P may be primarily used by ORP5 to deliver PS to LDs.

U2 - 10.1083/jcb.201905162

DO - 10.1083/jcb.201905162

M3 - Journal article

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

M1 - e201905162

ER -

ID: 291672750