Moesin and cortactin control actin-dependent multivesicular endosome biogenesis

Autor: Cameron C. Scott, Olivia Muriel, Jean Gruenberg, Alejandra Tomas
Rok vydání: 2016
Předmět:
Zdroj: Molecular Biology of the Cell
ISSN: 1939-4586
1059-1524
DOI: 10.1091/mbc.e15-12-0853
Popis: Moesin and cortactin on early endosomes are necessary for the formation of F-actin networks that mediate multivesicular endosome biogenesis and transport through the degradative pathway toward lysosomes. Presumably, this mechanism helps segregate recycling membranes from the maturing multivesicular endosomes.
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.
Databáze: OpenAIRE