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Sorting nexin 27 interactome in T‐lymphocytes identifies zona occludens‐2 dynamic redistribution at the immune synapse
Author(s) -
TelloLafoz María,
MartínezMartínez Gonzalo,
RodríguezRodríguez Cristina,
Albar Juan Pablo,
Huse Morgan,
Gharbi Severine,
Merida Isabel
Publication year - 2017
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12492
Subject(s) - sorting nexin , pdz domain , immunological synapse , interactome , biology , microbiology and biotechnology , endosome , retromer , immune system , t cell , immunology , genetics , t cell receptor , gene , intracellular
T Lymphocyte recognition of antigens leads to the formation of a highly organized structure termed immune synapse ( IS ) by analogy with the neuronals synapse. Sorting nexin 27 ( SNX27 ) controls the endosomal traffic of PSD95, Dlg1, ZO‐1 ( PDZ ) domain‐interacting proteins, and its alteration is associated with impaired synaptic function and neurological diseases. In T‐lymphocytes, SNX27 ‐positive vesicles polarize to the IS , the identity of SNX27 interactors in these conditions nonetheless remains unknown. Here we used proteomics to analyze the SNX27 interactome purified from IS ‐forming T cells, and confirmed the conserved nature of the SNX27 / WASH /retromer association in hematopoietic cells. Furthermore, our comparative interactome analysis of SNX27 wild‐type and a mutant‐deficient for PDZ cargo recognition identified the epithelial cell‐cell junction protein zona occludens‐2 ( ZO ‐2) as an IS component. Biochemistry and microscopy approaches in T cells confirmed SNX27 / ZO ‐2 PDZ ‐dependent interaction, and demonstrated its role controlling the dynamic localization of ZO ‐2 at the IS . This study broadens our knowledge of SNX27 function in T lymphocytes, and suggests that pathways that delimit polarized structures in nervous and epithelial systems also participate in IS regulation.