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The SH2 Domain Interaction Landscape

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78470

Olsen,  Jesper V.
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78356

Mann,  Matthias
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Tinti, M., Kiemer, L., Costa, S., Miller, M. L., Sacco, F., Olsen, J. V., et al. (2013). The SH2 Domain Interaction Landscape. CELL REPORTS, 3(4), 1293-1305. doi:10.1016/j.celrep.2013.03.001.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-4B18-E
Zusammenfassung
Members 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.