Journal
JOURNAL OF CELL SCIENCE
Volume 125, Issue 24, Pages 6020-6029Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.109561
Keywords
Fc gamma receptor; Image analysis; Myosin 1G; Phagocytosis
Categories
Funding
- Centre for Integrative Systems Biology and Bioinformatics (CISBIO)
- Biotechnology and Biological Sciences Research Council [BB/I019987/1]
- Biotechnology and Biological Sciences Research Council [BB/I019987/1, BB/C519670/1] Funding Source: researchfish
- BBSRC [BB/I019987/1] Funding Source: UKRI
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Phagocytosis is the force-dependent complex cellular process by which immune cells engulf particles. Although there has been considerable progress in understanding ligand-receptor-induced actin polymerisation in pushing the membrane around the particle, significantly less is known about how localised contractile activities regulate cup closure in coordination with the actin cytoskeleton. Herein, we show that the unconventional class-I myosin, myosin 1G (Myo1G) is localised at phagocytic cups following Fc gamma-receptor (Fc gamma R) ligation in macrophages. This progressive recruitment is dependent on the activity of phosphoinositide 3-kinase and is particularly important for engulfment of large particles. Furthermore, point mutations in the conserved pleckstrin homology-like domain of Myo1G abolishes the localisation of the motor protein at phagocytic cups and inhibits engulfment downstream of Fc gamma R. Binding of Myo1G to both F-actin and phospholipids might enable cells to transport phospholipids towards the leading edge of cups and to facilitate localised contraction for cup closure.
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