ArticleMolecular and cellular biology1995
The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 135 citations in OpenAlex.
- p66Shc deletion confers apoptotic resistance to loss of EGFR-ERK signalling in neural stem cells.Cell death & disease · 2025Article
- Breast Cancer and Prolactin - New Mechanisms and Models.Endocrinology · 2022Review
- Low-Density Lipoprotein Receptor-Related Protein 8 at the Crossroad between Cancer and Neurodegeneration.International journal of molecular sciences · 2022Review
- A conformational sensor based on genetic code expansion reveals an autocatalytic component in EGFR activation.Nature communications · 2018Article
- Src homology 2 domains enhance tyrosine phosphorylationThe Journal of biological chemistry · 2018Article
- Article
- Functional aspects of the EGF-induced MAP kinase cascade: a complex self-organizing system approach.PloS one · 2014Article
- Molecular characterization of EGFR and EGFRvIII signaling networks in human glioblastoma tumor xenografts.Molecular & cellular proteomics : MCP · 2012Article
- The ShcA SH2 domain engages a 14-3-3/PI3'K signaling complex and promotes breast cancer cell survival.Oncogene · 2012Article
- Robust co-regulation of tyrosine phosphorylation sites on proteins reveals novel protein interactions.Molecular bioSystems · 2012Article
- Article
- Epidermal growth factor receptor mutation in combination with expression of MIG6 alters gefitinib sensitivity.BMC systems biology · 2011Article
- Receptor tyrosine kinase signaling favors a protumorigenic state in breast cancer cells by inhibiting the adaptive immune response.Cancer research · 2010Article
- Cyclooxygenase-2 prevents fas-induced liver injury through up-regulation of epidermal growth factor receptor.Hepatology (Baltimore, Md.) · 2009Article
- Epidermal growth factor receptor lacking C-terminal autophosphorylation sites retains signal transduction and high sensitivity to epidermal growth factor receptor tyrosine kinase inhibitor.Cancer science · 2009Article
- Neuronal migration and the role of reelin during early development of the cerebral cortex.Molecular neurobiology · 2004Review
- Sck is expressed in endothelial cells and participates in vascular endothelial growth factor-induced signaling.Oncogene · 2002Article
- The UV (Ribotoxic) stress response of human keratinocytes involves the unexpected uncoupling of the Ras-extracellular signal-regulated kinase signaling cascade from the activated epidermal growth factor receptor.Molecular and cellular biology · 2002Article
- Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: role of Grb2.Molecular and cellular biology · 2001Article
- Docking protein FRS2 links the protein tyrosine kinase RET and its oncogenic forms with the mitogen-activated protein kinase signaling cascade.Molecular and cellular biology · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shc is an SH2 domain protein that is tyrosine phosphorylated in cells stimulated with a variety of growth factors and cytokines. Once phosphorylated, Shc binds the Grb2-Sos complex, leading to Ras activation. Shc can interact with tyrosine-phosphorylated proteins by binding to phosphotyrosine in the context of an NPXpY motif, where pY is a phosphotyrosine. This is an unusual binding site for an SH2 domain protein whose binding specificity is usually controlled by residues carboxy terminal, not amino terminal, to the phosphotyrosine. Recently we identified a second region in Shc, named the phosphotyrosine interaction (PI) domain, and we have found it to be present in a variety of other cellular proteins. In this study we used a dephosphorylation protection assay, competition analysis with phosphotyrosine-containing synthetic peptides, and epidermal growth factor receptor (EGFR) mutants to determine the binding sites of the PI domain of Shc on the EGFR. We demonstrate that the PI domain of Shc binds the LXNPXpY motif that encompasses Y-1148 of the activated EGFR. We conclude that the PI domain imparts to Shc its ability to bind the NPXpY motif.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.