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| Mol. Syst. Biol. (2005); 1:2005.0008 | |
| Phosphotyrosine interactome of the ErbB-receptor kinase family- | |
| Schulze WX, Deng L, Mann M | |
| Department of Biochemistry and Molecular Biology, Center for Experimental Bioinformatics, University of Southern Denmark, Odense, Denmark- | |
| Abstract: Interactions between short modified peptide motifs and modular protein domains are central events in cell signal-transduction- We determined interaction partners to all cytosolic tyrosine residues of the four members of the ErbB-receptor family in an unbiased fashion by quantitative proteomics using pull-down experiments with pairs of phosphorylated and nonphosphorylated synthetic peptides- Each receptor had characteristic preferences for interacting proteins and most interaction partners had multiple binding sites on each receptor- EGFR and ErbB4 had several docking sites for Grb2, while ErbB3 was characterized by six binding sites for PI3K- We identified STAT5 as a direct binding partner to EGFR and ErbB4 and discovered new recognition motifs for Shc and STAT5- The overall pattern of interaction partners of EGFR and ErbB4 suggests similar roles during signaling through their respective ligands- Phosphorylation kinetics of several tyrosine resides was measured by mass spectrometry and correlated with interaction partner preference- Our results demonstrate that system-wide mapping of peptide-protein interactions sites is possible, and suggest shared and unique roles of ErbB-receptor family members in downstream signaling- | |
| [PUBMED: 16729043] |   |
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| BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9. |