Document Detail

The motor protein Myosin 1G functions in FcγR-mediated phagocytosis.
MedLine Citation:
PMID:  23038771     Owner:  NLM     Status:  Publisher    
Phagocytosis is the force-dependent complex cellular process by which immune cells engulf particles. Whilst there has been considerable progress in understanding ligand-receptor-induced actin polymerization in pushing the membrane around the particle, significantly less is known about how localized contractile activities regulate cup closure in coordination with the actin cytoskeleton. Herein, we show that the unconventional class-I myosin, Myosin 1G (Myo1G) is localized at phagocytic cups following Fcγ-receptor (FcγR) 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 localization of the motor protein at phagocytic cups and inhibits engulfment downstream of FcγR. Binding of Myo1G to both F-actin and phospholipids may enable cells to transport phospholipids towards the leading edge of cups and to facilitate localized contraction for cup closure.
Anna E Dart; Sylvain Tollis; Michael D Bright; Gad M Frankel; Robert G Endres
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-4
Journal Detail:
Title:  Journal of cell science     Volume:  -     ISSN:  1477-9137     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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