PLD-dependent phosphatidic acid microdomains are signaling platforms for podosome formation.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
05 03 2019
05 03 2019
Historique:
received:
27
07
2018
accepted:
22
01
2019
entrez:
7
3
2019
pubmed:
7
3
2019
medline:
29
9
2020
Statut:
epublish
Résumé
Local membrane phospholipid enrichment serves as docking platform for signaling proteins involved in many processes including cell adhesion and migration. Tissue-resident dendritic cells (DCs) assemble actomyosin-based structures called podosomes, which mediate adhesion and degradation of extracellular matrix for migration and antigen sampling. Recent evidence suggested the involvement of phospholipase D (PLD) and its product phosphatidic acid (PA) in podosome formation, but the spatiotemporal control of this process is poorly characterized. Here we determined the role of PLD1 and PLD2 isoforms in regulating podosome formation and dynamics in human primary DCs by combining PLD pharmacological inhibition with a fluorescent PA sensor and fluorescence microscopy. We found that ongoing PLD2 activity is required for the maintenance of podosomes, whereas both PLD1 and PLD2 control the early stages of podosome assembly. Furthermore, we captured the formation of PA microdomains accumulating at the membrane cytoplasmic leaflet of living DCs, in dynamic coordination with nascent podosome actin cores. Finally, we show that both PLD1 and PLD2 activity are important for podosome-mediated matrix degradation. Our results provide novel insight into the isoform-specific spatiotemporal regulation of PLD activity and further our understanding of the role of cell membrane phospholipids in controlling localized actin polymerization and cell protrusion.
Identifiants
pubmed: 30837487
doi: 10.1038/s41598-019-39358-0
pii: 10.1038/s41598-019-39358-0
pmc: PMC6401089
doi:
Substances chimiques
Actins
0
Phosphatidic Acids
0
Phospholipase D
EC 3.1.4.4
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3556Subventions
Organisme : NHLBI NIH HHS
ID : R01 HL119478
Pays : United States
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