The internalization signal and the phosphorylation site of transferrin receptor are distinct from the main basolateral sorting information

Détails

ID Serval
serval:BIB_83F12B4B8567
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The internalization signal and the phosphorylation site of transferrin receptor are distinct from the main basolateral sorting information
Périodique
EMBO Journal
Auteur⸱e⸱s
Dargemont  C., Le Bivic  A., Rothenberger  S., Iacopetta  B., Kuhn  L. C.
ISSN
0261-4189 (Print)
Statut éditorial
Publié
Date de publication
04/1993
Volume
12
Numéro
4
Pages
1713-21
Notes
In Vitro
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Apr
Résumé
Wild-type human transferrin receptor (hTfR), like endogenous canine receptor, is expressed almost exclusively (97%) at the basolateral membrane of transfected Madin-Darbey canine kidney (MDCK) cells. We investigated the role of two distinct features of the hTfR cytoplasmic domain, namely the endocytic signal and the unique phosphorylation site, in polarized cell surface delivery. Basolateral location was not altered by point mutation of Ser24-->Ala24, indicating that phosphorylation is not involved in vectorial sorting of hTfR. The steady state distribution of hTfR was partially affected by a deletion of 36 cytoplasmic residues encompassing the internalization sequence. However, 80% of the receptors were still basolateral. As assessed by pulse-chase experiments in combination with biotinylation, newly synthesized wild-type and deletion mutant receptors were directly sorted to the domain of their steady state residency. Although both receptors could bind human transferrin, endocytosis of the deletion mutant was strongly impaired at either surface. These data indicate that the predominant basolateral targeting signal of hTfR is independent of the internalization sequence.
Mots-clé
Amino Acid Sequence Animals Cell Compartmentation Cell Line Cell Polarity Cytoplasm/ultrastructure DNA Mutational Analysis Dogs Endocytosis Humans Microscopy, Electron Molecular Sequence Data Phosphoproteins/physiology/ultrastructure Phosphorylation Receptors, Transferrin/*physiology/ultrastructure Recombinant Proteins/metabolism/ultrastructure Sequence Deletion Structure-Activity Relationship Transfection Transferrin/*metabolism
Pubmed
Web of science
Création de la notice
25/01/2008 15:36
Dernière modification de la notice
20/08/2019 15:43
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