Vps11 and Vps18 of Vps-C membrane traffic complexes are E3 ubiquitin ligases and fine-tune signalling

Gregory Segala, Marcela A. Bennesch, Nastaran Mohammadi Ghahhari, Deo Prakash Pandey, Pablo C. Echeverria, François Karch, Robert K. Maeda and Didier Picard ()
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Gregory Segala: Université de Genève, Sciences III
Marcela A. Bennesch: Université de Genève, Sciences III
Nastaran Mohammadi Ghahhari: Université de Genève, Sciences III
Deo Prakash Pandey: Université de Genève, Sciences III
Pablo C. Echeverria: Université de Genève, Sciences III
François Karch: Université de Genève, Sciences III
Robert K. Maeda: Université de Genève, Sciences III
Didier Picard: Université de Genève, Sciences III

Nature Communications, 2019, vol. 10, issue 1, 1-15

Abstract: Abstract In response to extracellular signals, many signalling proteins associated with the plasma membrane are sorted into endosomes. This involves endosomal fusion, which depends on the complexes HOPS and CORVET. Whether and how their subunits themselves modulate signal transduction is unknown. We show that Vps11 and Vps18 (Vps11/18), two common subunits of the HOPS/CORVET complexes, are E3 ubiquitin ligases. Upon overexpression of Vps11/Vps18, we find perturbations of ubiquitination in signal transduction pathways. We specifically demonstrate that Vps11/18 regulate several signalling factors and pathways, including Wnt, estrogen receptor α (ERα), and NFκB. For ERα, we demonstrate that the Vps11/18-mediated ubiquitination of the scaffold protein PELP1 impairs the activation of ERα by c-Src. Thus, proteins involved in membrane traffic, in addition to performing their well-described role in endosomal fusion, fine-tune signalling in several different ways, including through ubiquitination.

Date: 2019
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DOI: 10.1038/s41467-019-09800-y

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