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PMID: 3479328 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Phosphorylation of the human transferrin receptor by protein kinase C is not required for endocytosis and recycling in mouse 3T3 cells.

The EMBO journal ·Vol. 6 ·No. 9 ·1987-09-00 ·Pages 2661-7

Zerial M, Suomalainen M, Zanetti-Schneider M, Schneider C, Garoff H

Abstract

We have investigated the role of phosphorylation in the endocytosis of the human transferrin receptor (TR) by replacing its phosphorylation site, Ser24, with Ala through site-directed mutagenesis of the TR cDNA. The TR Ala24 mutant expressed in mouse 3T3 cells was not phosphorylated, even following stimulation of protein kinase C by phorbol ester. However, in spite of this defect the mutant was efficiently endocytosed and recycled back to the plasma membrane with kinetics similar to those of TR and a control mutant TR Ala63. Thus, these results confirm earlier results by Davis et al. (1986, J. Biol. Chem., 261-9034-9041) that Ser24 of human TR is the phosphorylation site for protein kinase C but do not support a role of this modification as a signal for TR endocytosis and recycling.

MeSH Terms
Animals Cell Line Cells, Cultured Endocytosis Humans Mutation Phorbol 12,13-Dibutyrate Phorbol Esters/pharmacology Phosphorylation Protein Kinase C/metabolism Receptors, Transferrin/drug effects,genetics,metabolism Transferrin/metabolism
Chemicals
Phorbol Esters Receptors, Transferrin Transferrin Phorbol 12,13-Dibutyrate Protein Kinase C
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Zerial M
Cell Biology Programme, European Molecular Biology Laboratory, Heidelberg, FRG.
Suomalainen M
Zanetti-Schneider M
Schneider C
Garoff H
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1987-09-00
Pages
2661-7
Language
English
Region
England
NLM ID
8208664
PMCID
PMC553687
Subset
IM
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