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Evolutionary conservation of the WASH complex: An actin polymerization machine involved in endosomal fission

Emmanuel Derivery and Alexis Gautreau
Volume 3, Issue 3
May/June 2010

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WASH is the Arp2/3 activating protein that is localized at the surface of endosomes, where it induces the formation of branched actin networks. This activity of WASH favors, in collaboration with dynamin, the fission of transport intermediates from endosomes, and hence regulates endosomal trafficking of several cargos. We have purified a novel stable multiprotein complex containing WASH, the WASH complex, and we examine here the evolutionary conservation of its seven subunits across diverse eukaryotic phyla. This analysis supports the idea that the invention of the WASH complex has involved the incorporation of an independent complex, the CapZ α/β heterodimer, forming the so-called Capping Protein (CP), as illustrated by the yeasts S. cerevisiae and S. pombe, which possess the CP heterodimer but no other subunits of the WASH complex. The alignements of the orthologous genes that we have generated give a view on the conservation of the different subunits and on their organization into domains. Moreover, we propose here a unique nomenclature for the different subunits to prevent future confusions in the field.

Derivery E, Sousa C, Gautier JJ, Lombard B, Loew D, Gautreau A. 2009. The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex. Dev Cell. 17:712-23.


Authors

Emmanuel Derivery
Laboratoire d'Enzymologie et de Biochimie Structurales, Gif sur Yvette, France
Alexis Gautreau Corresponding author: alexis.gautreau@lebs.cnrs-gif.fr
Laboratoire d'Enzymologie et de Biochimie Structurales, Gif sur Yvette, France

This is an open-access article


 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.

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