β-Arrestin-Dependent Endocytosis of Proteinase-Activated Receptor 2 Is Required for Intracellular Targeting of Activated ERK1/2

Recently, a requirement for β-arrestin-mediated endocytosis in the activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) by several G protein-coupled receptors (GPCRs) has been proposed. However, the importance of this requirement for function of ERK1/2 is unknown. We report that ago...

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Veröffentlicht in:	The Journal of cell biology 2000-03, Vol.148 (6), p.1267-1281
Hauptverfasser:	DeFea, K. A., Zalevsky, J., Thoma, M. S., Déry, O., Mullins, R. D., Bunnett, N. W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Agonists Animals Antibodies Arrestins - physiology beta-Arrestins Calcium - metabolism Cell Division Cell Line Cell lines Cell Nucleus - physiology Cell Nucleus - ultrastructure Cells Cellular biology Cytosol Cytosol - physiology Cytosol - ultrastructure Endocytosis Enzyme Activation Enzymes HEK293 cells Humans Inurement Kinetics Microscopy, Confocal Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases - metabolism Models, Biological Mutagenesis Mutation Original Phosphorylation Proteins Rats Receptor, PAR-2 Receptors Receptors, Thrombin - genetics Receptors, Thrombin - physiology Recombinant Proteins - metabolism Transfection
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