Trpml controls actomyosin contractility and couples migration to phagocytosis in fly macrophages.
Actomyosin
/ genetics
Animals
Animals, Genetically Modified
Calcium
/ metabolism
Calcium Signaling
Cell Movement
Cytoskeleton
/ genetics
Drosophila Proteins
/ genetics
Drosophila melanogaster
/ genetics
Hemocytes
/ immunology
Lysosomes
/ genetics
Macrophages
/ immunology
Myosin Type II
/ genetics
Phagocytosis
R-SNARE Proteins
/ genetics
Time Factors
Transient Receptor Potential Channels
/ genetics
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:
02 03 2020
02 03 2020
Historique:
received:
03
06
2019
revised:
13
11
2019
accepted:
07
12
2019
entrez:
16
1
2020
pubmed:
16
1
2020
medline:
21
10
2020
Statut:
ppublish
Résumé
Phagocytes use their actomyosin cytoskeleton to migrate as well as to probe their environment by phagocytosis or macropinocytosis. Although migration and extracellular material uptake have been shown to be coupled in some immune cells, the mechanisms involved in such coupling are largely unknown. By combining time-lapse imaging with genetics, we here identify the lysosomal Ca2+ channel Trpml as an essential player in the coupling of cell locomotion and phagocytosis in hemocytes, the Drosophila macrophage-like immune cells. Trpml is needed for both hemocyte migration and phagocytic processing at distinct subcellular localizations: Trpml regulates hemocyte migration by controlling actomyosin contractility at the cell rear, whereas its role in phagocytic processing lies near the phagocytic cup in a myosin-independent fashion. We further highlight that Vamp7 also regulates phagocytic processing and locomotion but uses pathways distinct from those of Trpml. Our results suggest that multiple mechanisms may have emerged during evolution to couple phagocytic processing to cell migration and facilitate space exploration by immune cells.
Identifiants
pubmed: 31940424
pii: 133603
doi: 10.1083/jcb.201905228
pmc: PMC7055000
pii:
doi:
Substances chimiques
Drosophila Proteins
0
R-SNARE Proteins
0
TRPML protein, Drosophila
0
Transient Receptor Potential Channels
0
VAMP7 protein, Drosophila
0
Actomyosin
9013-26-7
Myosin Type II
EC 3.6.1.-
Calcium
SY7Q814VUP
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Video-Audio Media
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2020 Edwards-Jorquera et al.
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