Titre
Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Auteur(s)
Rothenberger, S.
Auteure/Auteur
Iacopetta, B. J.
Auteure/Auteur
Kuhn, L. C.
Auteure/Auteur
Liens vers les personnes
Liens vers les unités
ISSN
0092-8674
Statut éditorial
Publié
Date de publication
1987-05
Volume
49
Numéro
3
Première page
423
Dernière page/numéro d’article
31
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May 8
Research Support, Non-U.S. Gov't --- Old month value: May 8
Résumé
The transferrin receptor (TR) mediates cellular iron uptake by bringing about the endocytosis of transferrin. We investigated whether the cytoplasmic domain of 65 N-terminal amino acids or phosphorylated sites within this domain constitute a structure that is required for TR endocytosis. To test this hypothesis, we modified the cytoplasmic serine residues or introduced a deletion of 36 amino acids by in vitro mutagenesis of a cDNA expression vector for human TR. Upon expression in transfected mouse Ltk- cells, both the wild-type and phosphorylation site mutant receptors mediated transferrin internalization, whereas the truncated receptor did not. These results provide evidence that the cytoplasmic domain, or part of it, is essential for internalization of the TR, but argue against a role for receptor phosphorylation in endocytosis.
Sujets
PID Serval
serval:BIB_BE7E2107746A
PMID
Date de création
2008-01-25T13:36:46.478Z
Date de création dans IRIS
2025-05-21T02:57:41Z