Securin and separase modulate membrane traffic by affecting endosomal acidification.

Détails

ID Serval
serval:BIB_58131F2C2A2F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Securin and separase modulate membrane traffic by affecting endosomal acidification.
Périodique
Traffic
Auteur(s)
Bacac M., Fusco C., Planche A., Santodomingo J., Demaurex N., Leemann-Zakaryan R., Provero P., Stamenkovic I.
ISSN
1600-0854 (Electronic)
ISSN-L
1398-9219
Statut éditorial
Publié
Date de publication
2011
Volume
12
Numéro
5
Pages
615-626
Langue
anglais
Résumé
Securin and separase play a key role in sister chromatid separation during anaphase. However, a growing body of evidence suggests that in addition to regulating chromosome segregation, securin and separase display functions implicated in membrane traffic in Caenorhabditis elegans and Drosophila. Here we show that in mammalian cells both securin and separase associate with membranes and that depletion of either protein causes robust swelling of the trans-Golgi network (TGN) along with the appearance of large endocytic vesicles in the perinuclear region. These changes are accompanied by diminished constitutive protein secretion as well as impaired receptor recycling and degradation. Unexpectedly, cells depleted of securin or separase display defective acidification of early endosomes and increased membrane recruitment of vacuolar (V-) ATPase complexes, mimicking the effect of the specific V-ATPase inhibitor Bafilomycin A1. Taken together, our findings identify a new functional role of securin and separase in the modulation of membrane traffic and protein secretion that implicates regulation of V-ATPase assembly and function.
Pubmed
Web of science
Création de la notice
26/04/2011 13:26
Dernière modification de la notice
20/08/2019 14:11
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