Sorting mechanisms regulating membrane protein traffic in the apical transcytotic pathway of polarized MDCK cells.

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Etat: Serval
Version: de l'auteur
ID Serval
serval:BIB_3EBEBE83249A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Sorting mechanisms regulating membrane protein traffic in the apical transcytotic pathway of polarized MDCK cells.
Périodique
The Journal of cell biology
Auteur(s)
Gibson A., Futter C.E., Maxwell S., Allchin E.H., Shipman M., Kraehenbuhl J.P., Domingo D., Odorizzi G., Trowbridge I.S., Hopkins C.R.
ISSN
0021-9525
Statut éditorial
Publié
Date de publication
1998
Peer-reviewed
Oui
Volume
143
Numéro
1
Pages
81-94
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. - Publication Status: ppublish
Résumé
The transcytotic pathway followed by the polymeric IgA receptor (pIgR) carrying its bound ligand (dIgA) from the basolateral to the apical surface of polarized MDCK cells has been mapped using morphological tracers. At 20 degreesC dIgA-pIgR internalize to interconnected groups of vacuoles and tubules that comprise the endosomal compartment and in which they codistribute with internalized transferrin receptors (TR) and epidermal growth factor receptors (EGFR). Upon transfer to 37 degreesC the endosome vacuoles develop long tubules that give rise to a distinctive population of 100-nm-diam cup-shaped vesicles containing pIgR. At the same time, the endosome gives rise to multivesicular endosomes (MVB) enriched in EGFR and to 60-nm-diam basolateral vesicles. The cup-shaped vesicles carry the dIgA/pIgR complexes to the apical surface where they exocytose. Using video microscopy and correlative electron microscopy to study cells grown thin and flat we show that endosome vacuoles tubulate in response to dIgA/pIgR but that the tubules contain TR as well as pIgR. However, we show that TR are removed from these dIgA-induced tubules via clathrin-coated buds and, as a result, the cup-shaped vesicles to which the tubules give rise become enriched in dIgA/pIgR. Taken together with the published information available on pIgR trafficking signals, our observations suggest that the steady-state concentrations of TR and unoccupied pIgR on the basolateral surface of polarized MDCK cells are maintained by a signal-dependent, clathrin-based sorting mechanism that operates along the length of the transcytotic pathway. We propose that the differential sorting of occupied receptors within the MDCK endosome is achieved by this clathrin-based mechanism continuously retrieving receptors like TR from the pathways that deliver pIgR to the apical surface and EGFR to the lysosome.
Mots-clé
Animals, Cell Line, Cell Membrane, Cell Polarity, Dogs, Endocytosis, Endosomes, Immunoglobulin A, Kidney, Kinetics, Membrane Proteins, Microscopy, Electron, Microscopy, Video, Receptor, Epidermal Growth Factor, Receptors, Fc, Receptors, Transferrin
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 16:05
Dernière modification de la notice
08/05/2019 17:31
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