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


Journal

The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356

Informations de publication

Date de publication:
06 01 2020
Historique:
received: 22 05 2019
revised: 17 09 2019
accepted: 03 10 2019
pubmed: 28 10 2019
medline: 28 7 2020
entrez: 27 10 2019
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 31653673
pii: jcb.201905162
doi: 10.1083/jcb.201905162
pmc: PMC7039201
pii:
doi:

Substances chimiques

Minor Histocompatibility Antigens 0
Phosphatidylinositol Phosphates 0
Phospholipid Transfer Proteins 0
Receptors, Steroid 0
oxysterol binding protein 0
phosphatidylinositol 4-phosphate 0
Phosphotransferases (Alcohol Group Acceptor) EC 2.7.1.-
phosphatidylinositol phosphate 4-kinase EC 2.7.1.67

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Commentaires et corrections

Type : CommentIn

Informations de copyright

© 2019 Du et al.

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Auteurs

Ximing Du (X)

School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

Linkang Zhou (L)

State Key Laboratory of Membrane Biology and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.

Yvette Celine Aw (YC)

School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

Hoi Yin Mak (HY)

School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

Yanqing Xu (Y)

School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

James Rae (J)

Centre for Microscopy and Microanalysis, Institute of Molecular Bioscience, University of Queensland, St. Lucia, Australia.

Wenmin Wang (W)

State Key Laboratory of Membrane Biology and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.

Armella Zadoorian (A)

School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

Sarah E Hancock (SE)

School of Medical Sciences, The University of New South Wales, Sydney, Australia.

Brenna Osborne (B)

School of Medical Sciences, The University of New South Wales, Sydney, Australia.

Xiang Chen (X)

Institute of Molecular Enzymology, Soochow University, Suzhou, Jiangsu, China.

Jia-Wei Wu (JW)

Institute of Molecular Enzymology, Soochow University, Suzhou, Jiangsu, China.

Nigel Turner (N)

School of Medical Sciences, The University of New South Wales, Sydney, Australia.

Robert G Parton (RG)

Centre for Microscopy and Microanalysis, Institute of Molecular Bioscience, University of Queensland, St. Lucia, Australia.

Peng Li (P)

State Key Laboratory of Membrane Biology and Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.

Hongyuan Yang (H)

School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

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Classifications MeSH