Threonine Phosphorylation Diverts Internalized Epidermal Growth Factor Receptors from a Degradative Pathway to the Recycling Endosome
Authors:
- Iris AlroyIris Alroy
- Hadassa WatermanHWHadassa Waterman
- Eyal D. SchejterESEyal D. Schejter
- Chaya BrodieCBChaya Brodie
- Jean GruenbergJGJean Gruenberg
- Yosef YardenYYYosef Yarden
Open Access
- 1 August 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (34) , 26178-26186
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- High-affinity Binding of Epidermal Growth Factor (EGF) to EGF Receptor Is Disrupted by Overexpression of Mutant Dynamin (K44A)Journal of Biological Chemistry, 1998
- Control of EGF Receptor Signaling by Clathrin-Mediated EndocytosisScience, 1996
- Lysosomal Targeting of Epidermal Growth Factor Receptors via a Kinase-dependent Pathway Is Mediated by the Receptor Carboxyl-terminal Residues 1022-1123Journal of Biological Chemistry, 1996
- Signal-Dependent Membrane Protein Trafficking in the Endocytic PathwayAnnual Review of Cell Biology, 1993
- Endocytosis of growth factor receptorsBioEssays, 1993
- GROWTH FACTOR RECEPTOR TYROSINE KINASESAnnual Review of Biochemistry, 1988
- Epidermal growth factor (EGF) promotes phosphorylation at threonine-654 of the EGF receptor: possible role of protein kinase C in homologous regulation of the EGF receptor.Journal of Cell Biology, 1986
- Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanismsCell, 1986
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONSAnnals of the New York Academy of Sciences, 1949