ArticleMolecular and cellular biology1992
The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment.
Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 87 citations in OpenAlex.
- Sinner or Saint?: Nck Adaptor Proteins in Vascular Biology.Frontiers in cell and developmental biology · 2021Review
- An EHBP-1-SID-3-DYN-1 axis promotes membranous tubule fission during endocytic recycling.PLoS genetics · 2020Article
- Recruitment of the adaptor protein Nck to PECAM-1 couples oxidative stress to canonical NF-κB signaling and inflammation.Science signaling · 2015Article
- Phosphatase of regenerating liver 3 (PRL3) provokes a tyrosine phosphoproteome to drive prometastatic signal transduction.Molecular & cellular proteomics : MCP · 2013Article
- Nck2 promotes human melanoma cell proliferation, migration and invasion in vitro and primary melanoma-derived tumor growth in vivo.BMC cancer · 2011Article
- Proteomic analysis of tyrosine phosphorylation during human liver transplantation.Proteome science · 2007Article
- Use of double-stranded RNA-mediated interference to determine the substrates of protein tyrosine kinases and phosphatases.The Biochemical journal · 2002Article
- Review
- Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3'-kinase binding.The Biochemical journal · 2001Article
- alphaPIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinase.Oncogene · 1999Article
- Angiotensin II stimulates serine phosphorylation of the adaptor protein Nck: physical association with the serine/threonine kinases Pak1 and casein kinase I.The Biochemical journal · 1999Article
- Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways.Molecular biology of the cell · 1998Article
- Requirement for phospholipase C-gamma1 enzymatic activity in growth factor-induced mitogenesis.Molecular and cellular biology · 1998Article
- Expression of mutated Nck SH2/SH3 adaptor respecifies mesodermal cell fate in Xenopus laevis development.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac.The Biochemical journal · 1997Article
- CrkII signals from epidermal growth factor receptor to Ras.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins.Molecular and cellular biology · 1995Article
- Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex.Molecular biology of the cell · 1995Article
- Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains.Molecular and cellular biology · 1995Article
- Binding of NCK to SOS and activation of ras-dependent gene expression.Molecular and cellular biology · 1995Article
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Authors and funding
2 authors.
Funding
Abstract
In the course of our investigation of phospholipase C (PLC)-gamma 1 phosphorylation by using a set of anti-PLC-gamma 1 monoclonal antibodies (P.-G. Suh, S. H. Ryu, W. C. Choi, K.-Y. Lee, and S. G. Rhee, J. Biol. Chem. 263:14497-14504, 1988), we found that some of these antibodies directly recognize a 47-kDa protein. We show here that this 47-kDa protein is identical to the SH2/SH3-containing protein Nck (J. M. Lehmann, G. Riethmuller, and J. P. Johnson, Nucleic Acids Res. 18:1048, 1990). Nck was found to be constitutively phosphorylated on serine in resting NIH 3T3 cells. Platelet-derived growth factor (PDGF) treatment led to increased Nck phosphorylation on both tyrosine and serine. Nck was also found to be phosphorylated on tyrosine in epidermal growth factor (EGF)-treated A431 cells and in v-Src-transformed NIH 3T3 cells. Multiple sites of serine phosphorylation were detected in Nck from resting cells, and no novel sites were found upon PDGF or EGF treatment. A single major tyrosine phosphorylation site was found in Nck in both PDGF- and EGF-treated cells and in v-Src-transformed cells. This same tyrosine was phosphorylated in vitro by purified PDGF and EGF receptors and also by pp60c-src. We compared the phosphorylation of Nck and PLC-gamma 1 in several cell lines transformed by oncogenes with different modes of transformation. Although PLC-gamma 1 and Nck have significant amino acid identity, particularly in their SH3 regions, and both associate with growth factor receptors in a ligand-dependent manner, they were not always phosphorylated on tyrosine in a coincident manner.
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