scholarly journals Boosting ER folding capacity reduces UPR activation and intracellular accumulation of human kidney anion exchanger 1 in S. cerevisiae

Yeast ◽  
2021 ◽  
Author(s):  
Xiaobing Li ◽  
Emmanuelle Cordat ◽  
Manfred J. Schmitt ◽  
Björn Becker
Keyword(s):  
Anion Exchanger ◽  
Human Kidney ◽  
Intracellular Accumulation ◽  
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

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

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

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.

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

A Novel Mutation in the Anion Exchanger 1 Gene Is Associated With Familial Distal Renal Tubular Acidosis and Nephrocalcinosis

PEDIATRICS ◽  
2003 ◽  
Vol 112 (6) ◽  
pp. 1361-1367 ◽  
Author(s):  
L. Cheidde ◽  
T. C. Vieira ◽  
P. R. M. Lima ◽  
S. T. O. Saad ◽  
I. P. Heilberg
Keyword(s):  
Renal Tubular Acidosis ◽  
Anion Exchanger ◽  
Novel Mutation ◽  
Distal Renal Tubular Acidosis ◽  
Anion Exchanger 1 ◽  
Renal Tubular
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