Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site

Détails

ID Serval
serval:BIB_BE7E2107746A
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site
Périodique
Cell
Auteur(s)
Rothenberger  S., Iacopetta  B. J., Kuhn  L. C.
ISSN
0092-8674 (Print)
Statut éditorial
Publié
Date de publication
05/1987
Volume
49
Numéro
3
Pages
423-31
Notes
Journal Article
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.
Mots-clé
Amino Acid Sequence Animals Cell Line Cytoplasm/metabolism DNA/metabolism *Endocytosis Genetic Vectors Humans Kinetics Mutation Phosphorylation Receptors, Transferrin/*genetics/metabolism Transferrin/metabolism
Pubmed
Web of science
Création de la notice
25/01/2008 15:36
Dernière modification de la notice
20/08/2019 16:32
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