TGN38 recycles basolaterally in polarized Madin-Darby canine kidney cells

Sorting of newly synthesized plasma membrane proteins to the apical or basolateral surface domains of polarized cells is currently thought to take place within the trans-Golgi network (TGN). To explore the relationship between protein localization to the TGN and sorting to the plasma membrane in pol...

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Bibliographic Details
Published in:Molecular biology of the cell 1994-10, Vol.5 (10), p.1093-1103
Main Authors: Rajasekaran, A K, Humphrey, J S, Wagner, M, Miesenböck, G, Le Bivic, A, Bonifacino, J S, Rodriguez-Boulan, E
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biomarkers
Cell Line
Cell Membrane - metabolism
Cell Polarity
Dogs
Fluorescent Antibody Technique
Glycoproteins
Golgi Apparatus - metabolism
Kidney - cytology
Kidney - metabolism
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Membrane Proteins
Molecular Sequence Data
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
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Summary:Sorting of newly synthesized plasma membrane proteins to the apical or basolateral surface domains of polarized cells is currently thought to take place within the trans-Golgi network (TGN). To explore the relationship between protein localization to the TGN and sorting to the plasma membrane in polarized epithelial cells, we have expressed constructs encoding the TGN marker, TGN38, in Madin-Darby canine kidney (MDCK) cells. We report that TGN38 is predominantly localized to the TGN of these cells and recycles via the basolateral membrane. Analyses of the distribution of Tac-TGN38 chimeric proteins in MDCK cells suggest that the cytoplasmic domain of TGN38 has information leading to both TGN localization and cycling through the basolateral surface. Mutations of the cytoplasmic domain that disrupt TGN localization also lead to nonpolarized delivery of the chimeric proteins to both surface domains. These results demonstrate an apparent equivalence of basolateral and TGN localization determinants and support an evolutionary relationship between TGN and plasma membrane sorting processes.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.5.10.1093