Lipid-associated PML structures assemble nuclear lipid droplets containing CCTα and Lipin1.
Animals
CHO Cells
Cell Nucleus
/ metabolism
Choline-Phosphate Cytidylyltransferase
/ metabolism
Cricetulus
Fatty Acids
/ metabolism
Humans
Lipid Droplets
/ metabolism
Nuclear Envelope
/ metabolism
Oleic Acid
/ metabolism
Phosphatidate Phosphatase
/ metabolism
Phosphatidylcholines
/ chemistry
Promyelocytic Leukemia Protein
/ metabolism
Journal
Life science alliance
ISSN: 2575-1077
Titre abrégé: Life Sci Alliance
Pays: United States
ID NLM: 101728869
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
22
04
2020
revised:
13
05
2020
accepted:
14
05
2020
entrez:
29
5
2020
pubmed:
29
5
2020
medline:
15
7
2021
Statut:
epublish
Résumé
Nuclear lipid droplets (nLDs) form on the inner nuclear membrane by a mechanism involving promyelocytic leukemia (PML), the protein scaffold of PML nuclear bodies. We report that PML structures on nLDs in oleate-treated U2OS cells, referred to as lipid-associated PML structures (LAPS), differ from canonical PML nuclear bodies by the relative absence of SUMO1, SP100, and DAXX. These nLDs were also enriched in CTP:phosphocholine cytidylyltransferase α (CCTα), the phosphatidic acid phosphatase Lipin1, and DAG. Translocation of CCTα onto nLDs was mediated by its α-helical M-domain but was not correlated with its activator DAG. High-resolution imaging revealed that CCTα and LAPS occupied distinct polarized regions on nLDs. PML knockout U2OS (PML KO) cells lacking LAPS had a 40-50% reduction in nLDs with associated CCTα, and residual nLDs were almost devoid of Lipin1 and DAG. As a result, phosphatidylcholine and triacylglycerol synthesis was inhibited in PML KO cells. We conclude that in response to excess exogenous fatty acids, LAPS are required to assemble nLDs that are competent to recruit CCTα and Lipin1.
Identifiants
pubmed: 32461215
pii: 3/8/e202000751
doi: 10.26508/lsa.202000751
pmc: PMC7266991
pii:
doi:
Substances chimiques
Fatty Acids
0
Phosphatidylcholines
0
Promyelocytic Leukemia Protein
0
PML protein, human
143220-95-5
Oleic Acid
2UMI9U37CP
Choline-Phosphate Cytidylyltransferase
EC 2.7.7.15
PCYT1A protein, human
EC 2.7.7.15
LPIN1 protein, human
EC 3.1.3.4
Phosphatidate Phosphatase
EC 3.1.3.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : CIHR
ID : PJT62390
Pays : Canada
Informations de copyright
© 2020 Lee et al.
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