A Restricted Set of Apical Proteins Recycle Through the Trans-Golgi Network in MDCK Cells

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 1989 Nov 1

PMID 2510995

Citations 7

Authors

A W Brandli

K Simons

Affiliations

Soon will be listed here.

Abstract

Sorting of newly synthesized proteins destined for the apical plasma membrane takes place in the trans-Golgi network (TGN) in MDCK cells. This process is most likely receptor mediated and requires components that recycle between both compartments. We have developed an assay to detect apical proteins that recycle through the sialyltransferase-containing TGN. Cell surface glycoproteins were exogalactosylated apically using a mutant cell line derived from MDCK, MDCKII-RCAr. The mutant exhibits impaired galactosylation of glycoconjugates and thereby allows maximal incorporation of exogenously added galactose in the presence of galactosyltransferase. Upon reculture at 37 degrees C, a time-dependent increase of sialylated apical surface glycoproteins was observed by lectin binding as well as by the sialic acid-specific NaIO4/NaB[3H]4 labeling technique. This indicates that some galactosylated surface molecules had returned to the TGN. Recycling through the TGN was blocked, if exogalactosylated cells were incubated at 20 degrees C. Two-dimensional gel electrophoresis identified three apical proteins which recycle through the TGN, suggesting that this pathway is selective for a subset of the apical surface proteins.

Citing Articles

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TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain.

Bos K, Wraight C, Stanley K EMBO J. 1993; 12(5):2219-28.

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Annexin XIIIb: a novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane.

Fiedler K, Lafont F, Parton R, Simons K J Cell Biol. 1995; 128(6):1043-53.

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Selective reentry of recycling cell surface glycoproteins to the biosynthetic pathway in human hepatocarcinoma HepG2 cells.

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Transcytosis in MDCK cells: identification of glycoproteins transported bidirectionally between both plasma membrane domains.

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