The Phosphotyrosine Peptide Binding Specificity of Nck1 and Nck2 Src Homology 2 Domains
Open Access
- 1 June 2006
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 281 (26), 18236-18245
- https://doi.org/10.1074/jbc.m512917200
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high‐affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ‐RGS3 proteinEuropean Journal of Biochemistry, 2004
- Tyr-298 in ephrinB1 is critical for an interaction with the Grb4 adaptor proteinBiochemical Journal, 2004
- Nckβ Interacts with Tyrosine-Phosphorylated Disabled 1 and Redistributes in Reelin-Stimulated NeuronsMolecular and Cellular Biology, 2003
- The Murine Nck SH2/SH3 Adaptors Are Important for the Development of Mesoderm-Derived Embryonic Structures and for Regulating the Cellular Actin NetworkMolecular and Cellular Biology, 2003
- The Nck family of adapter proteinsCellular Signalling, 2002
- The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signalsNature, 2001
- Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cellsNature, 2001
- Nckβ Adapter Regulates Actin Polymerization in NIH 3T3 Fibroblasts in Response to Platelet-Derived Growth Factor bbMolecular and Cellular Biology, 2000
- Identification of Grb4/Nckβ, a Src Homology 2 and 3 Domain-containing Adapter Protein Having Similar Binding and Biological Properties to NckJournal of Biological Chemistry, 1999
- Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3Nucleic Acids Research, 1990