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

Article Details

Citation

Rothenberger S, Iacopetta BJ, Kuhn LC

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

Cell. 1987 May 8;49(3):423-31.

PubMed ID
3568132 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Transferrin receptor protein 1P02786Details