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2017 ; 28
(7
): 890-897
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Vamp-7-dependent secretion at the immune synapse regulates antigen extraction and
presentation in B-lymphocytes
#MMPMID28179460
Obino D
; Diaz J
; Sáez JJ
; Ibañez-Vega J
; Sáez PJ
; Alamo M
; Lankar D
; Yuseff MI
Mol Biol Cell
2017[Apr]; 28
(7
): 890-897
PMID28179460
show ga
Recognition of surface-tethered antigens (Ags) by B-cells leads to the formation
of an immune synapse that promotes Ag uptake for presentation onto MHC-II
molecules. Extraction of immobilized Ags at the immune synapse of B-cells relies
on the local secretion of lysosomes, which are recruited to the Ag contact site
by polarization of their microtubule network. Although conserved polarity
proteins have been implicated in coordinating cytoskeleton remodeling with
lysosome trafficking, the cellular machinery associated with lysosomal vesicles
that regulates their docking and secretion at the synaptic interface has not been
defined. Here we show that the v-SNARE protein Vamp-7 is associated with
Lamp-1(+) lysosomal vesicles, which are recruited and docked at the center of the
immune synapse of B-cells. A decrease in Vamp-7 expression does not alter
lysosome transport to the synaptic interface but impairs their local secretion, a
defect that compromises the ability of B-cells to extract, process, and present
immobilized Ag. Thus our results reveal that B-cells rely on the SNARE protein
Vamp-7 to promote the local exocytosis of lysosomes at the immune synapse, which
is required for efficient Ag extraction and presentation.