Role of Adaptor Proteins and Clathrin in the Trafficking of Human Kidney Anion Exchanger 1 (kAE1) to the Cell Surface

Traffic ◽  
2014 ◽  
Vol 15 (7) ◽  
pp. 788-802 ◽  
Author(s):  
Mutita Junking ◽  
Nunghathai Sawasdee ◽  
Natapol Duangtum ◽  
Boonyarit Cheunsuchon ◽  
Thawornchai Limjindaporn ◽  
...  
Keyword(s):  
Cell Surface ◽  
Anion Exchanger ◽  
Human Kidney ◽  
Adaptor Proteins ◽  
Anion Exchanger 1

scholarly journals Analysis of the interaction between human kidney anion exchanger 1 and kanadaptin using yeast two-hybrid systems

2006 ◽  
Vol 29 (1) ◽  
pp. 14-22
Author(s):  
Phonphimon Wongthida ◽  
Varaporn Akkarapatumwong ◽  
Thawornchai Limjindaporn ◽  
Saranya Kittanakom ◽  
Thitima Keskanokwong ◽  
...  
Keyword(s):  
Hybrid Systems ◽  
Anion Exchanger ◽  
Human Kidney ◽  
Yeast Two Hybrid ◽  
Anion Exchanger 1 ◽  
Two Hybrid

Impaired trafficking of distal renal tubular acidosis mutants of the human kidney anion exchanger kAE1

2002 ◽  
Vol 282 (5) ◽  
pp. F810-F820 ◽  
Author(s):  
Janne A. Quilty ◽  
Jing Li ◽  
Reinhart A. Reithmeier
Keyword(s):  
Cell Surface ◽  
Renal Tubular Acidosis ◽  
Anion Exchanger ◽  
Human Kidney ◽  
Distal Renal Tubular Acidosis ◽  
Dominant Negative ◽  
Cell Surface Expression ◽  
Dominant Negative Effect ◽  
Inherited Disease ◽  
Renal Tubular

Distal renal tubular acidosis (dRTA) is an inherited disease characterized by the failure of the kidneys to appropriately acidify urine and is associated with mutations in the anion exchanger (AE)1 gene. The effect of the R589H dRTA mutation on the expression of the human erythroid AE1 and the truncated kidney form (kAE1) was examined in transfected human embryonic kidney 293 cells. AE1, AE1 R589H, and kAE1 were present at the cell surface, whereas kAE1 R589H was located primarily intracellularly as shown by immunofluorescence, cell surface biotinylation, N-glycosylation, and anion transport assays. Coexpression of kAE1 R589H reduced the cell surface expression of kAE1 and AE1 by a dominant-negative effect, due to heterodimer formation. The mutant AE1 and kAE1 bound to an inhibitor affinity resin, suggesting that they were not grossly misfolded. Other mutations at R589 also prevented the formation of the cell surface form of kAE1, indicating that this conserved arginine residue is important for proper trafficking. The R589H dRTA mutation creates a severe trafficking defect in kAE1 but not in erythroid AE1.

scholarly journals Palmitoylation is not required for trafficking of human anion exchanger 1 to the cell surface

2004 ◽  
Vol 378 (3) ◽  
pp. 1015-1021 ◽  
Author(s):  
Joanne C. CHEUNG ◽  
Reinhart A. F. REITHMEIER
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Palmitic Acid ◽  
Anion Exchanger ◽  
Cell Surface Expression ◽  
Co2 Removal ◽  
Anion Exchanger 1 ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
293 Cells

AE1 (anion exchanger 1) is a glycoprotein found in the plasma membrane of erythrocytes, where it mediates the electroneutral exchange of chloride and bicarbonate, a process important in CO2 removal from tissues. It had been previously shown that human AE1 purified from erythrocytes is covalently modified at Cys-843 in the membrane domain with palmitic acid. In this study, the role of Cys-843 in human AE1 trafficking was investigated by expressing various AE1 and Cys-843Ala (C843A) mutant constructs in transiently transfected HEK-293 cells. The AE1 C843A mutant was expressed to a similar level to AE1. The rate of N-glycan conversion from high-mannose into complex form in a glycosylation mutant (N555) of AE1 C843A, and thus the rate of trafficking from the endoplasmic reticulum to the Golgi, were comparable with that of AE1 (N555). Like AE1, AE1 C843A could be biotinylated at the cell surface, indicating that a cysteine residue at position 843 is not required for cell-surface expression of the protein. The turnover rate of AE1 C843A was not significantly different from AE1. While other proteins could be palmitoylated, labelling of transiently transfected HEK-293 cells or COS7 cells with [3H]palmitic acid failed to produce any detectable AE1 palmitoylation. These results suggest that AE1 is not palmitoylated in HEK-293 or COS7 cells and can traffic to the plasma membrane.

scholarly journals Topology of transmembrane segments 1–4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesis

2005 ◽  
Vol 390 (1) ◽  
pp. 137-144 ◽  
Author(s):  
Joanne C. Cheung ◽  
Jing Li ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Plasma Membrane ◽  
Anion Exchanger ◽  
Physiological Role ◽  
Mutant Form ◽  
Extracellular Loop ◽  
Anion Exchanger 1 ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells ◽  
Transmembrane Segments

Human AE1 (anion exchanger 1), or Band 3, is an abundant membrane glycoprotein found in the plasma membrane of erythrocytes. The physiological role of the protein is to carry out chloride/bicarbonate exchange across the plasma membrane, a process that increases the carbon-dioxide-carrying capacity of blood. To study the topology of TMs (transmembrane segments) 1–4, a series of scanning N-glycosylation mutants were created spanning the region from EC (extracellular loop) 1 to EC2 in full-length AE1. These constructs were expressed in HEK-293 (human embryonic kidney) cells, and their N-glycosylation efficiencies were determined. Unexpectedly, positions within putative TMs 2 and 3 could be efficiently glycosylated. In contrast, the same positions were very poorly glycosylated when present in mutant AE1 with the SAO (Southeast Asian ovalocytosis) deletion (ΔA400–A408) in TM1. These results suggest that the TM2–3 region of AE1 may become transiently exposed to the endoplasmic reticulum lumen during biosynthesis, and that there is a competition between proper folding of the region into the membrane and N-glycosylation at introduced sites. The SAO deletion disrupts the proper integration of TMs 1–2, probably leaving the region exposed to the cytosol. As a result, engineered N-glycosylation acceptor sites in TM2–3 could not be utilized by the oligosaccharyltransferase in this mutant form of AE1. The properties of TM2–3 suggest that these segments form a re-entrant loop in human AE1.

No Evidence for Role of Common Anion Exchanger 1 Mutations on the Severity Difference in HB E-β-Thalassemia Disease in Northeast Thailand

2013 ◽  
Vol 13 (2) ◽  
pp. 99-103
Author(s):  
Lalitpatch Ngouprommin ◽  
Nattaya Sae-ung ◽  
Supan Fucharoen ◽  
Goonnapa Fucharoen ◽  
Kanokwan Sanchaisuriya ◽  
...  
Keyword(s):  
Anion Exchanger ◽  
Northeast Thailand ◽  
Anion Exchanger 1 ◽  
Hb E ◽  
Common Anion

scholarly journals Human kidney anion exchanger 1 localisation in MDCK cells is controlled by the phosphorylation status of two critical tyrosines

2008 ◽  
Vol 121 (20) ◽  
pp. 3422-3432 ◽  
Author(s):  
R. C. Williamson ◽  
A. C. N. Brown ◽  
W. J. Mawby ◽  
A. M. Toye
Keyword(s):  
Anion Exchanger ◽  
Mdck Cells ◽  
Human Kidney ◽  
Anion Exchanger 1
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