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Human kidney anion exchanger 1 interacts with adaptor-related protein complex 1 μ1A (AP-1 mu1A)

Authors :
Sawasdee, Nunghathai
Junking, Mutita
Ngaojanlar, Piengpaga
Sukomon, Nattakan
Ungsupravate, Duangporn
Limjindaporn, Thawornchai
Akkarapatumwong, Varaporn
Noisakran, Sansanee
Yenchitsomanus, Pa-thai
Source :
Biochemical & Biophysical Research Communications. Oct2010, Vol. 401 Issue 1, p85-91. 7p.
Publication Year :
2010

Abstract

Abstract: Kidney anion exchanger 1 (kAE1) mediates chloride (Cl−) and bicarbonate (HCO3 −) exchange at the basolateral membrane of kidney α-intercalated cells. Impaired trafficking of kAE1 leads to defect of the Cl−/HCO3 − exchange at the basolateral membrane and failure of proton (H+) secretion at the apical membrane, causing a kidney disease – distal renal tubular acidosis (dRTA). To gain a better insight into kAE1 trafficking, we searched for proteins physically interacting with the C-terminal region of kAE1 (Ct-kAE1), which contains motifs crucial for intracellular trafficking, by a yeast two-hybrid (Y2H) system. An adaptor-related protein complex 1 μ1A (AP-1 mu1A) subunit was found to interact with Ct-kAE1. The interaction between either Ct-kAE1 or full-length kAE1 and AP-1 mu1A were confirmed in human embryonic kidney (HEK) 293T by co-immunoprecipitation, affinity co-purification, co-localization, yellow fluorescent protein (YFP)-based protein fragment complementation assay (PCA) and GST pull-down assay. The interacting site for AP-1 mu1A on Ct-kAE1 was found to be Y904DEV907, a subset of YXXØ motif. Interestingly, suppression of endogenous AP-1 mu1A in HEK 293T by small interfering RNA (siRNA) decreased membrane localization of kAE1 and increased its intracellular accumulation, suggesting for the first time that AP-1 mu1A is involved in the kAE1 trafficking of kidney α-intercalated cells. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0006291X
Volume :
401
Issue :
1
Database :
Academic Search Index
Journal :
Biochemical & Biophysical Research Communications
Publication Type :
Academic Journal
Accession number :
54368377
Full Text :
https://doi.org/10.1016/j.bbrc.2010.09.015