Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site
- 1 May 1987
- Vol. 49 (3), 423-431
- https://doi.org/10.1016/0092-8674(87)90295-9
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosisCell, 1986
- The possible link between receptor phosphorylation and internalizationTrends in Pharmacological Sciences, 1985
- Receptor-Mediated Endocytosis: Concepts Emerging from the LDL Receptor SystemAnnual Review of Cell Biology, 1985
- Internalization-defective LDL receptors produced by genes with nonsense and frameshift mutations that truncate the cytoplasmic domainCell, 1985
- Phorbol esters and horseradish peroxidase stimulate pinocytosis and redirect the flow of pinocytosed fluid in macrophages.The Journal of cell biology, 1985
- The appearance and internalization of transferrin receptors at the margins of spreading human tumor cellsCell, 1985
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- Selection and properties of a mouse L-cell transformant expressing human transferrin receptorNature, 1983
- Murine cell surface transferrin receptor: Studies with an anti‐receptor monoclonal antibodyJournal of Cellular Physiology, 1982
- Inhibition of reticulocyte iron uptake by NH4Cl and CH3NH2Biochimica et Biophysica Acta (BBA) - Biomembranes, 1981