Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 27, Issue 21, Pages 3305-3316Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E15-12-0853
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Funding
- Swiss National Science Foundation
- Swiss Sinergia Programme
- Polish-Swiss Research Programme [PSPB-094/2010]
- National Centre of Competence in Research in Chemical Biology from the Swiss SystemsX.ch initiative
- LipidX from the Swiss SystemsX.ch initiative
- European Molecular Biology Organization [ALTF-516-2012]
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We used in vivo and in vitro strategies to study the mechanisms of multivesicular endosome biogenesis. We found that, whereas annexinA2 and ARP2/3 mediate F-actin nucleation and branching, respectively, the ERM protein moesin supports the formation of F-actin networks on early endosomes. We also found that moesin plays no role during endocytosis and recycling to the plasma membrane but is absolutely required, much like actin, for early-to-late-endosome transport and multivesicular endosome formation. Both actin network formation in vitro and early-to-late endosome transport in vivo also depend on the F-actin-binding protein cortactin. Our data thus show that moesin and cortactin are necessary for formation of F-actin networks that mediate endosome biogenesis or maturation and transport through the degradative pathway. We propose that the primary function of endosomal F-actin is to control the membrane remodeling that accompanies endosome biogenesis. We also speculate that this mechanism helps segregate tubular and multivesicular membranes along the recycling and degradation pathways, respectively.
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