The SH2 Domain Interaction Landscape
| Autor: | Lars Kiemer, Matthias Mann, Nikolaj Blom, Martina Carducci, Luisa Castagnoli, Gianni Cesareni, Stefano Costa, Jesper V. Olsen, Francesca Langone, Kazuya Machida, Christopher M. Thompson, Martin L. Miller, Mike Schutkowski, Michele Tinti, Christopher T. Workman, Søren Brunak, Serena Paoluzi, Francesca Sacco, Bruce J. Mayer |
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| Rok vydání: | 2013 |
| Předmět: |
Phosphopeptides
Proteome Protein domain Protein Array Analysis Protein Tyrosine Phosphatase Non-Receptor Type 11 Context (language use) Computational biology Protein tyrosine phosphatase Biology SH2 domain Article General Biochemistry Genetics and Molecular Biology Protein–protein interaction src Homology Domains 03 medical and health sciences Tandem Mass Spectrometry Interaction network Humans Amino Acid Sequence Protein Interaction Maps Phosphorylation Databases Protein Extracellular Signal-Regulated MAP Kinases Phosphotyrosine lcsh:QH301-705.5 Chromatography High Pressure Liquid 030304 developmental biology 0303 health sciences 030302 biochemistry & molecular biology Settore BIO/18 - Genetica ROC Curve lcsh:Biology (General) Biochemistry biology.protein GRB2 Phosphotyrosine-binding domain HeLa Cells |
| Zdroj: | CELL REPORTS Cell Reports, Vol 3, Iss 4, Pp 1293-1305 (2013) Tinti, M, Kiemer, L, Costa, S, Miller, M L, Sacco, F, Olsen, J, Carducci, M, Paoluzi, S, Langone, F, Workman, C, Blom, N, Machida, K, Thompson, C M, Schutkowski, M, Brunak, S, Mann, M, Mayer, B J, Castagnoli, L & Cesareni, G 2013, ' The SH2 Domain Interaction Landscape ', Cell Reports, vol. 3, no. 4, pp. 1293-1305 . https://doi.org/10.1016/j.celrep.2013.03.001 |
| ISSN: | 2211-1247 |
| DOI: | 10.1016/j.celrep.2013.03.001 |
| Popis: | SummaryMembers of the SH2 domain family modulate signal transduction by binding to short peptides containing phosphorylated tyrosines. Each domain displays a distinct preference for the sequence context of the phosphorylated residue. We have developed a high-density peptide chip technology that allows for probing of the affinity of most SH2 domains for a large fraction of the entire complement of tyrosine phosphopeptides in the human proteome. Using this technique, we have experimentally identified thousands of putative SH2-peptide interactions for more than 70 different SH2 domains. By integrating this rich data set with orthogonal context-specific information, we have assembled an SH2-mediated probabilistic interaction network, which we make available as a community resource in the PepspotDB database. A predicted dynamic interaction between the SH2 domains of the tyrosine phosphatase SHP2 and the phosphorylated tyrosine in the extracellular signal-regulated kinase activation loop was validated by experiments in living cells. |
| Databáze: | OpenAIRE |
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