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Dynamin A, Myosin IB and Abp1 couple phagosome maturation to F-actin binding

Authors
Patel, Devang
Kratzke, Ramona
Krüger, Julia
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Published in Traffic. 2012, vol. 13, no. 1, p. 120-30
Abstract The role of actin, class I myosins and dynamin in endocytic uptake processes is well characterized, but their role during endo-phagosomal membrane trafficking and maturation is less clear. In Dictyostelium, knockout of myosin IB (myoB) leads to a defect in membrane protein recycling from endosomes back to the plasma membrane. Here, we show that actin plays a central role in the morphology and function of the endocytic pathway. Indeed, latrunculin B (LatB) induces endosome tubulation, a phenotype also observed in dynamin A (dymA)-null cells. Knockout of dymA impairs phagosome acidification, whereas knockout of myoB delays reneutralization, a phenotype mimicked by a low dose of LatB. As a read out for actin-dependent processes during maturation, we monitored the capacity of purified phagosomes to bind F-actin in vitro, and correlated this with the presence of actin-binding and membrane-trafficking proteins. Phagosomes isolated from myoB-null cells showed an increased binding to F-actin, especially late phagosomes. In contrast, early phagosomes from dymA-null cells showed reduced binding to F-actin while late phagosomes were unaffected. We provide evidence that Abp1 is the main F-actin-binding protein in this assay and is central for the interplay between DymA and MyoB during phagosome maturation.
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PMID: 22008230
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GOPALDASS, Navin Andréw et al. Dynamin A, Myosin IB and Abp1 couple phagosome maturation to F-actin binding. In: Traffic, 2012, vol. 13, n° 1, p. 120-30. https://archive-ouverte.unige.ch/unige:18866

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Deposited on : 2012-03-19

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