Phosphorylation of the human transferrin receptor by protein kinase C is not required for endocytosis and recycling in mouse 3T3 cells.
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.
D000818:Animals; D002460:Cell Line; D002478:Cells, Cultured; D004705:Endocytosis; D006801:Humans; D009154:Mutation; D015240:Phorbol 12,13-Dibutyrate; D010703:Phorbol Esters / Q000494:pharmacology; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011990:Receptors, Transferrin / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism
D010703:Phorbol Esters; D011990:Receptors, Transferrin; D014168:Transferrin; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C