BibTex format

author = {Martzoukou, O and Karachaliou, M and Yalelis, V and Leung, J and Byrne, B and Amillis, S and Diallinas, G},
doi = {10.1016/j.jmb.2015.05.021},
journal = {Journal of Molecular Biology},
pages = {2679--2696},
title = {Oligomerization of the UapA purine transporter Is critical for ER-exit, plasma membrane localization and turnover},
url = {},
volume = {427},
year = {2015}

RIS format (EndNote, RefMan)

AB - Central to the process of transmembrane cargo trafficking is the successful folding and exit from the ER (endoplasmic reticulum) through packaging in COPII vesicles. Here, we use the UapA purine transporter of Aspergillus nidulans to investigate the role of cargo oligomerization in membrane trafficking. We show that UapA oligomerizes (at least dimerizes) and that oligomerization persists upon UapA endocytosis and vacuolar sorting. Using a validated bimolecular fluorescence complementation assay, we provide evidence that a UapA oligomerization is associated with ER-exit and turnover, as ER-retained mutants due to either modification of a Tyr-based N-terminal motif or partial misfolding physically associate but do not associate properly. Co-expression of ER-retained mutants with wild-type UapA leads to in trans plasma membrane localization of the former, confirming that oligomerization initiates in the ER. Genetic suppression of an N-terminal mutation in the Tyr motif and mutational analysis suggest that transmembrane α-helix 7 affects the oligomerization interface. Our results reveal that transporter oligomerization is essential for membrane trafficking and turnover and is a common theme in fungi and mammalian cells.
AU - Martzoukou,O
AU - Karachaliou,M
AU - Yalelis,V
AU - Leung,J
AU - Byrne,B
AU - Amillis,S
AU - Diallinas,G
DO - 10.1016/j.jmb.2015.05.021
EP - 2696
PY - 2015///
SN - 1089-8638
SP - 2679
TI - Oligomerization of the UapA purine transporter Is critical for ER-exit, plasma membrane localization and turnover
T2 - Journal of Molecular Biology
UR -
UR -
UR -
VL - 427
ER -