RT info:eu-repo/semantics/article
T1 Securin and Separase Modulate Membrane Traffic by Affecting Endosomal Acidification
A1 Bacac, Marina
A1 Fusco, Carlo
A1 Planche, Anne
A1 Santodomingo, Jaime
A1 Demaurex, Nicolas
A1 Leemann‐Zakaryan, Ruzanna
A1 Provero, Paolo
A1 Stamenkovic, Ivan
K1 endosome, acidification, V-ATPase, securin, separase
AB 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.
PB Wiley
SN 1398-9219
YR 2011
FD 2011
LK https://uvadoc.uva.es/handle/10324/65926
UL https://uvadoc.uva.es/handle/10324/65926
LA eng
NO Traffic, May 2011, vol. 12, n. 5, p. 615-26.
NO Producción Científica
DS UVaDOC
RD 28-nov-2024