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

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

Dominant and Recessive Distal Renal Tubular Acidosis Mutations of Kidney Anion Exchanger 1 Induce Distinct Trafficking Defects in MDCK Cells

Traffic ◽  
2005 ◽  
Vol 7 (2) ◽  
pp. 117-128 ◽  
Author(s):  
Emmanuelle Cordat ◽  
Saranya Kittanakom ◽  
Pa-thai Yenchitsomanus ◽  
Jing Li ◽  
Kai Du ◽  
...  
Keyword(s):  
Renal Tubular Acidosis ◽  
Anion Exchanger ◽  
Mdck Cells ◽  
Distal Renal Tubular Acidosis ◽  
Anion Exchanger 1 ◽  
Trafficking Defects ◽  
Renal Tubular

Human kidney anion exchanger 1 interacts with kinesin family member 3B (KIF3B)

2011 ◽  
Vol 413 (1) ◽  
pp. 69-74 ◽  
Author(s):  
Natapol Duangtum ◽  
Mutita Junking ◽  
Nunghathai Sawasdee ◽  
Boonyarit Cheunsuchon ◽  
Thawornchai Limjindaporn ◽  
...  
Keyword(s):  
Family Member ◽  
Anion Exchanger ◽  
Human Kidney ◽  
Anion Exchanger 1 ◽  
Kinesin Family

scholarly journals Saccharomyces cerevisiae: First Steps to a Suitable Model System To Study the Function and Intracellular Transport of Human Kidney Anion Exchanger 1

mSphere ◽  
2020 ◽  
Vol 5 (1) ◽  
Author(s):  
Hasib A. M. Sarder ◽  
Xiaobing Li ◽  
Charlotta Funaya ◽  
Emmanuelle Cordat ◽  
Manfred J. Schmitt ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Anion Exchanger ◽  
Intracellular Transport ◽  
Human Kidney ◽  
Model System ◽  
Full Length ◽  
Anion Exchanger 1 ◽  
Content Type ◽  
Renal Tubular

ABSTRACT Saccharomyces cerevisiae has been frequently used to study biogenesis, functionality, and intracellular transport of various renal proteins, including ion channels, solute transporters, and aquaporins. Specific mutations in genes encoding most of these renal proteins affect kidney function in such a way that various disease phenotypes ultimately occur. In this context, human kidney anion exchanger 1 (kAE1) represents an important bicarbonate/chloride exchanger which maintains the acid-base homeostasis in the human body. Malfunctions in kAE1 lead to a pathological phenotype known as distal renal tubular acidosis (dRTA). Here, we evaluated the potential of baker's yeast as a model system to investigate different cellular aspects of kAE1 physiology. For the first time, we successfully expressed yeast codon-optimized full-length versions of tagged and untagged wild-type kAE1 and demonstrated their partial localization at the yeast plasma membrane (PM). Finally, pH and chloride measurements further suggest biological activity of full-length kAE1, emphasizing the potential of S. cerevisiae as a model system for studying trafficking, activity, and/or degradation of mammalian ion channels and transporters such as kAE1 in the future. IMPORTANCE Distal renal tubular acidosis (dRTA) is a common kidney dysfunction characterized by impaired acid secretion via urine. Previous studies revealed that α-intercalated cells of dRTA patients express mutated forms of human kidney anion exchanger 1 (kAE1) which result in inefficient plasma membrane targeting or diminished expression levels of kAE1. However, the precise dRTA-causing processes are inadequately understood, and alternative model systems are helpful tools to address kAE1-related questions in a fast and inexpensive way. In contrast to a previous study, we successfully expressed full-length kAE1 in Saccharomyces cerevisiae. Using advanced microscopy techniques as well as different biochemical and functionality assays, plasma membrane localization and biological activity were confirmed for the heterologously expressed anion transporter. These findings represent first important steps to use the potential of yeast as a model organism for studying trafficking, activity, and degradation of kAE1 and its mutant variants in the future.

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

2010 ◽  
Vol 401 (1) ◽  
pp. 85-91 ◽  
Author(s):  
Nunghathai Sawasdee ◽  
Mutita Junking ◽  
Piengpaga Ngaojanlar ◽  
Nattakan Sukomon ◽  
Duangporn Ungsupravate ◽  
...  
Keyword(s):  
Anion Exchanger ◽  
Protein Complex ◽  
Human Kidney ◽  
Related Protein ◽  
Anion Exchanger 1

scholarly journals Trafficking defects of the Southeast Asian ovalocytosis deletion mutant of anion exchanger 1 membrane proteins

2005 ◽  
Vol 392 (3) ◽  
pp. 425-434 ◽  
Author(s):  
Joanne C. Cheung ◽  
Emmanuelle Cordat ◽  
Reinhart A. F. Reithmeier
Keyword(s):  
Cell Surface ◽  
Anion Exchanger ◽  
Mdck Cells ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Intercalated Cells ◽  
Anion Exchanger 1 ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
293 Cells

Human AE1 (anion exchanger 1) is a membrane glycoprotein found in erythrocytes and as a truncated form (kAE1) in the BLM (basolateral membrane) of α-intercalated cells of the distal nephron, where they carry out electroneutral chloride/bicarbonate exchange. SAO (Southeast Asian ovalocytosis) is a dominant inherited haematological condition arising from deletion of Ala400–Ala408 in AE1, resulting in a misfolded and transport-inactive protein present in the ovalocyte membrane. Heterozygotes with SAO are able to acidify their urine, without symptoms of dRTA (distal renal tubular acidosis) that can be associated with mutations in kAE1. We examined the effect of the SAO deletion on stability and trafficking of AE1 and kAE1 in transfected HEK-293 (human embryonic kidney) cells and kAE1 in MDCK (Madin–Darby canine kidney) epithelial cells. In HEK-293 cells, expression levels and stabilities of SAO proteins were significantly reduced, and no mutant protein was detected at the cell surface. The intracellular retention of AE1 SAO in transfected HEK-293 cells suggests that erythroid-specific factors lacking in HEK-293 cells may be required for cell-surface expression. Although misfolded, SAO proteins could form heterodimers with the normal proteins, as well as homodimers. In MDCK cells, kAE1 was localized to the cell surface or the BLM after polarization, while kAE1 SAO was retained intracellularly. When kAE1 SAO was co-expressed with kAE1 in MDCK cells, kAE1 SAO was largely retained intracellularly; however, it also co-localized with kAE1 at the cell surface. We propose that, in the kidney of heterozygous SAO patients, dimers of kAE1 and heterodimers of kAE1 SAO and kAE1 traffic to the BLM of α-intercalated cells, while homodimers of kAE1 SAO are retained in the endoplasmic reticulum and are rapidly degraded. This results in sufficient cell-surface expression of kAE1 to maintain adequate bicarbonate reabsorption and proton secretion without dRTA.

Transmembrane protein 139 (TMEM139) interacts with human kidney isoform of anion exchanger 1 (kAE1)

2015 ◽  
Vol 463 (4) ◽  
pp. 706-711
Author(s):  
Nalin-on Nuiplot ◽  
Mutita Junking ◽  
Natapol Duangtum ◽  
Sasiprapa Khunchai ◽  
Nunghathai Sawasdee ◽  
...  
Keyword(s):  
Anion Exchanger ◽  
Transmembrane Protein ◽  
Human Kidney ◽  
Anion Exchanger 1

Anion exchanger 1 in human kidney and oncocytoma differs from erythroid AE1 in its NH2 terminus

1993 ◽  
Vol 265 (6) ◽  
pp. F813-F821 ◽  
Author(s):  
A. Kollert-Jons ◽  
S. Wagner ◽  
S. Hubner ◽  
H. Appelhans ◽  
D. Drenckhahn
Keyword(s):  
Anion Exchanger ◽  
Sequence Data ◽  
Collecting Duct ◽  
Basolateral Membrane ◽  
Human Kidney ◽  
Renal Oncocytoma ◽  
Intercalated Cells ◽  
Anion Exchanger 1 ◽  
Dna Sequence Data ◽  
Acid Secreting

Acid-secreting intercalated cells of the kidney collecting duct and tumor cells of renal oncocytoma express an anion exchanger that is immunologically related but not identical to the chloride-bicarbonate anion exchanger of erythrocytes (AE1). In this study, we have mapped the binding site of a monoclonal antibody against erythroid AE1 that does not react with either intercalated cells or oncocytoma. The epitope is located close to the NH2 terminus of AE1, indicating that AE1 in intercalated cells and oncocytoma differs in its NH2 terminus from erythroid AE1. This conclusion was supported by an antibody directed against residues 1-14 of erythroid AE1 that does not react with intercalated cells in oncocytoma. Polymerase chain reaction performed with mRNA from a human kidney revealed that the sequence containing the codons for Met-1 and Met-33 in erythroid mRNA is missing in the kidney transcript, whereas the sequence coding for Met-66 is present. DNA sequence data derived from cloning the 5' end of the human kidney AE1 mRNA clearly showed that the 5' untranslated region comprises part of intron 3, the complete exon 4 that is followed by exon 5 containing Met-66 as the site of translation initiation. Altogether, the results indicate that AE1 in the human kidney is an amino-terminally truncated form of erythroid AE1 that is restricted to the basolateral membrane domain of the acid-secreting intercalated cells of the collecting duct and is also expressed in oncocytoma.

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