scholarly journals Multiple cytoplasmic signals direct the intracellular trafficking of chicken kidney AE1 anion exchangers in MDCK cells

2002 ◽  
Vol 116 (4) ◽  
pp. 655-663 ◽  
Author(s):  
T. L. Adair-Kirk
Keyword(s):  
Intracellular Trafficking ◽  
Mdck Cells ◽  
Anion Exchangers ◽  
Chicken Kidney ◽  
Cytoplasmic Signals

scholarly journals Intracellular Trafficking of Variant Chicken Kidney Ae1 Anion Exchangers

1999 ◽  
Vol 147 (6) ◽  
pp. 1237-1248 ◽  
Author(s):  
Tracy L. Adair-Kirk ◽  
Kathleen H. Cox ◽  
John V. Cox
Keyword(s):  
Amino Acids ◽  
Actin Cytoskeleton ◽  
Anion Exchanger ◽  
Apical Membrane ◽  
Mdck Cells ◽  
Basolateral Membrane ◽  
Critical Role ◽  
Anion Exchangers ◽  
Tyrosine Residues ◽  
Chicken Kidney

The variant chicken kidney AE1 anion exchangers differ only at the NH2 terminus of their cytoplasmic domains. Transfection studies have indicated that the variant chicken AE1-4 anion exchanger accumulates in the basolateral membrane of polarized MDCK kidney epithelial cells, while the AE1-3 variant, which lacks the NH2-terminal 63 amino acids of AE1-4, primarily accumulates in the apical membrane. Mutagenesis studies have shown that the basolateral accumulation of AE1-4 is dependent upon two tyrosine residues at amino acids 44 and 47 of the polypeptide. Interestingly, either of these tyrosines is sufficient to direct efficient basolateral sorting of AE1-4. However, in the absence of both tyrosine residues, AE1-4 accumulates in the apical membrane of MDCK cells. Pulse–chase studies have shown that after delivery to the cell surface, newly synthesized AE1-4 is recycled to the Golgi where it acquires additional N-linked sugar modifications. This Golgi recycling activity is dependent upon the same cytoplasmic tyrosine residues that are required for the basolateral sorting of this variant transporter. Furthermore, mutants of AE1-4 that are defective in Golgi recycling are unable to associate with the detergent insoluble actin cytoskeleton and are rapidly turned over. These studies, which represent the first description of tyrosine-dependent cytoplasmic sorting signal for a type III membrane protein, have suggested a critical role for the actin cytoskeleton in regulating AE1 anion exchanger localization and stability in this epithelial cell type.

scholarly journals Cytoplasmic Signals Mediate Apical Early Endosomal Targeting of Endotubin in MDCK Cells

Traffic ◽  
2001 ◽  
Vol 2 (7) ◽  
pp. 487-500 ◽  
Author(s):  
K. E. Gokay ◽  
R. S. Young ◽  
J. M. Wilson
Keyword(s):  
Mdck Cells ◽  
Cytoplasmic Signals

scholarly journals Tracking Endocytosis and Intracellular Trafficking of Epitope-tagged Syntaxin 3 by Antibody Feeding in Live, Polarized MDCK Cells

BIO-PROTOCOL ◽  
2018 ◽  
Vol 8 (3) ◽  
Author(s):  
Adrian Giovannone ◽  
Elena Reales ◽  
Pallavi Bhattaram ◽  
Alberto Fraile-Ramos ◽  
Thomas Weimbs
Keyword(s):  
Intracellular Trafficking ◽  
Mdck Cells ◽  
Syntaxin 3

Variant chicken AE1 anion exchangers possess divergent NH(2)-terminal cytoplasmic domains

1995 ◽  
Vol 268 (3) ◽  
pp. F503-F513 ◽  
Author(s):  
K. H. Cox ◽  
J. V. Cox
Keyword(s):  
Amino Acids ◽  
Anion Exchanger ◽  
Rna Splicing ◽  
Transcription Initiation ◽  
Primary Transcript ◽  
Anion Exchangers ◽  
Transcriptional Initiation ◽  
Terminal Amino ◽  
Chicken Kidney

Immunoblotting analyses have demonstrated that antibodies specific for the chicken erythroid AE1 anion exchanger recognize multiple polypeptides ranging in size from approximately 95 to 112 kDa in chicken kidney. To determine the origin of this diversity, we have cloned and characterized the kidney AE1 anion exchangers. These studies have shown that the kidney AE1 polypeptides are encoded by at least three transcripts, AE1-3, AE1-4, and AE1-5, which differ from the erythroid AE1-1 and AE1-2 transcripts in the sequences present at their 5'-ends. The AE1-3 and AE1-5 transcripts encode predicted polypeptides of approximately 94 kDa, which are identical to the erythroid AE1-1 anion exchanger except for the absence of the 78 NH(2)-terminal amino acids of the AE1-1 polypeptide. In contrast, the AE1-4 transcript encodes a predicted polypeptide of approximately 101 kDa, whose 21 NH(2)-terminal amino acids are unique. Characterization of the AE1 cDNAs has suggested that the AE1-3 and AE1-4 transcripts are generated by alternative splicing of a single primary transcript, while DNA blotting analyses have shown that the putative transcription initiation sites of the variant AE1-4 and AE1-5 transcripts lie several kilobases downstream of the transcription initiation sites of the erythroid AE1-1 and AE1-2 transcripts. These results suggest that the pattern of accumulation of the variant kidney AE1 anion exchangers is regulated by a complex pattern of alternative transcriptional initiation and differential RNA splicing.

Cr(VI) RETENTION CAPACITY AND SELECTIVITY OF SOME STRONG AND WEAK BASE ANION EXCHANGERS

2004 ◽  
Vol 3 (3) ◽  
pp. 221-230 ◽  
Author(s):  
Ion Untea ◽  
Cristina Orbeci ◽  
Elena Tudorache ◽  
Violeta Neagu
Keyword(s):  
Weak Base ◽  
Anion Exchangers ◽  
Retention Capacity
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