A β-Arrestin-dependent Scaffold Is Associated with Prolonged MAPK Activation in Pseudopodia during Protease-activated Receptor-2-induced Chemotaxis
Open Access
- 1 September 2003
- journal article
- Published by Elsevier BV
- Vol. 278 (36), 34418-34426
- https://doi.org/10.1074/jbc.m300573200
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- ERK and RhoA Differentially Regulate Pseudopodia Growth and Retraction during ChemotaxisJournal of Biological Chemistry, 2003
- β-Arrestin2 Is Critically Involved in CXCR4-mediated Chemotaxis, and This Is Mediated by Its Enhancement of p38 MAPK ActivationPublished by Elsevier BV ,2002
- Suppression of Integrin Activation by Activated Ras or Raf Does Not Correlate with Bulk Activation of ERK MAP KinaseMolecular Biology of the Cell, 2002
- Defective lymphocyte chemotaxis in β-arrestin2- and GRK6-deficient miceProceedings of the National Academy of Sciences of the United States of America, 2002
- Expanding roles for β-arrestins as scaffolds and adapters in GPCR signaling and traffickingCurrent Opinion in Cell Biology, 2001
- Tissue factor- and factor X-dependent activation of protease-activated receptor 2 by factor VIIaProceedings of the National Academy of Sciences of the United States of America, 2000
- Phosphorylation of WAVE Downstream of Mitogen-activated Protein Kinase SignalingJournal of Biological Chemistry, 1999
- A Cell's Sense of DirectionScience, 1999
- Proteinase-activated receptors: a growing family of heptahelical receptors for thrombin, trypsin and tryptaseBiochemical Society Transactions, 1999
- Regulation of Cell Motility by Mitogen-activated Protein KinaseThe Journal of cell biology, 1997