scholarly journals Clathrin and AP1 are required for apical sorting of glycosyl phosphatidyl inositol‐anchored proteins in biosynthetic and recycling routes in Madin‐Darby canine kidney cells

Traffic ◽  
2018 ◽  
Vol 19 (3) ◽  
pp. 215-228 ◽  
Author(s):  
Guillaume A. Castillon ◽  
Patricia Burriat‐Couleru ◽  
Daniel Abegg ◽  
Nina Criado Santos ◽  
Reika Watanabe
Keyword(s):  
Phosphatidyl Inositol ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Apical Sorting ◽  
Darby Canine Kidney ◽  
Canine Kidney

scholarly journals Direct apical sorting of rat liver dipeptidylpeptidase IV expressed in Madin-Darby canine kidney cells.

1991 ◽  
Vol 266 (36) ◽  
pp. 24428-24432
Author(s):  
J.E. Casanova ◽  
Y. Mishumi ◽  
Y. Ikehara ◽  
A.L. Hubbard ◽  
K.E. Mostov
Keyword(s):  
Rat Liver ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Dipeptidylpeptidase Iv ◽  
Apical Sorting ◽  
Darby Canine Kidney ◽  
Canine Kidney

N-glycans as apical targeting signals in polarized epithelial cells.

2005 ◽  
Vol 72 ◽  
pp. 39-45 ◽  
Author(s):  
Paula Urquhart ◽  
Susan Pang ◽  
Nigel M. Hooper
Keyword(s):  
Epithelial Cells ◽  
Kidney Cells ◽  
Apical Surface ◽  
Madin Darby Canine Kidney ◽  
Targeting Signals ◽  
Polarized Epithelial Cells ◽  
Apical Sorting ◽  
Darby Canine Kidney ◽  
Canine Kidney

MDCK (Madin-Darby canine kidney) cells represent a good model of polarized epithelium to investigate the signals involved in the apical targeting of proteins. As reported previously, GPI (glycosylphosphatidylinositol) anchors mediate the apical sorting of proteins in polarized epithelial cells through their interaction with lipid rafts. However, using a naturally N-glycosylated and GPI-anchored protein, we found that the GPI anchor does not influence the targeting of the protein. It is, in fact, the N-glycans that signal the protein to the apical surface. In the present review, the role of N-glycans and GPI anchors as apical signals is discussed along with the putative mechanisms involved.

scholarly journals SpecificN-Glycans Direct Apical Delivery of Transmembrane, but Not Soluble or Glycosylphosphatidylinositol-anchored Forms of Endolyn in Madin-Darby Canine Kidney Cells

2004 ◽  
Vol 15 (3) ◽  
pp. 1407-1416 ◽  
Author(s):  
Beth A. Potter ◽  
Gudrun Ihrke ◽  
Jennifer R. Bruns ◽  
Kelly M. Weixel ◽  
Ora A. Weisz
Keyword(s):  
Transmembrane Protein ◽  
Site Directed Mutagenesis ◽  
Kidney Cells ◽  
Apical Surface ◽  
Glycosidase Inhibitors ◽  
Madin Darby Canine Kidney ◽  
Reporter Protein ◽  
Apical Sorting ◽  
Darby Canine Kidney ◽  
Canine Kidney

The sialomucin endolyn is a transmembrane protein with a unique trafficking pattern in polarized Madin-Darby canine kidney cells. Despite the presence of a cytoplasmic tyrosine motif that, in isolation, is sufficient to mediate basolateral sorting of a reporter protein, endolyn predominantly traverses the apical surface en route to lysosomes. Apical delivery of endolyn is disrupted in tunicamycin-treated cells, implicating a role for N-glycosylation in apical sorting. Site-directed mutagenesis of endolyn's eight N-glycosylation sites was used to identify two N-glycans that seem to be the major determinants for efficient apical sorting of the protein. In addition, apical delivery of endolyn was disrupted when terminal processing of N-glycans was blocked using glycosidase inhibitors. Missorting of endolyn occurred independently of the presence or absence of the basolateral sorting signal, because apical delivery was also inhibited by tunicamycin when the cytoplasmic tyrosine motif was mutated. However, we found that apical secretion of a soluble mutant of endolyn was N-glycan independent, as was delivery of glycosylphosphatidylinositol-anchored endolyn. Thus, specific N-glycans are only essential for the apical sorting of transmembrane endolyn, suggesting fundamental differences in the mechanisms by which soluble, glycosylphosphatidylinositol-anchored, and transmembrane proteins are sorted.

scholarly journals Inhibition by brefeldin A of protein secretion from the apical cell surface of Madin-Darby canine kidney cells.

1991 ◽  
Vol 266 (27) ◽  
pp. 17729-17732 ◽  
Author(s):  
S.H. Low ◽  
S.H. Wong ◽  
B.L. Tang ◽  
P. Tan ◽  
V.N. Subramaniam ◽  
...  
Keyword(s):  
Cell Surface ◽  
Protein Secretion ◽  
Apical Cell ◽  
Brefeldin A ◽  
Kidney Cells ◽  
Madin Darby Canine Kidney ◽  
Darby Canine Kidney ◽  
Canine Kidney
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