Tyrosyl Phosphorylation of Shp2 Is Required for Normal ERK Activation in Response to Some, but Not All, Growth Factors
Open Access
- 1 October 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (43) , 41677-41684
- https://doi.org/10.1074/jbc.m306461200
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Site-Specific Incorporation of a Phosphotyrosine Mimetic Reveals a Role for Tyrosine Phosphorylation of SHP-2 in Cell SignalingMolecular Cell, 2001
- Shp-2 mediates v-Src-induced morphological changes and activation of the anti-apoptotic protein kinase AktOncogene, 2000
- Shp‐2 Specifically Regulates Several Tyrosine‐Phosphorylated Proteins in Brain‐Derived Neurotrophic Factor SignalJournal of Neurochemistry, 2000
- Src Family Tyrosine Kinases and Growth Factor SignalingExperimental Cell Research, 2000
- Src family kinases are required for integrin but not PDGFR signal transductionThe EMBO Journal, 1999
- The Shp-2 Tyrosine Phosphatase Has Opposite Effects in Mediating the Activation of Extracellular Signal-regulated and c-Jun NH2-terminal Mitogen-activated Protein KinasesJournal of Biological Chemistry, 1998
- A Grb2-associated docking protein in EGF- and insulin-receptor signallingNature, 1996
- Protein-tyrosine Phosphatase 1D Modulates Its Own State of Tyrosine PhosphorylationJournal of Biological Chemistry, 1995
- PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiationCurrent Biology, 1994
- SH2-Containing Phosphotyrosine Phosphatase as a Target of Protein-Tyrosine KinasesScience, 1993