The SH2 Domain Interaction Landscape

Michele Tinti, Lars Kiemer, Stefano Costa, Martin Lee Miller, Francesca Sacco, Jesper Olsen, Martina Carducci, Serena Paoluzi, Francesca Langone, Christopher Workman, Nikolaj Blom, Kazuya Machida, Christopher M. Thompson, Mike Schutkowski, Søren Brunak, Matthias Mann, Bruce J. Mayer, Luisa Castagnoli, Gianni Cesareni

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    Cells respond to growth factors and additional external and internal molecular cues by changing their tyrosine phosphorylation profile. This in turn triggers the modulation of complexes that read and process the information. Cesareni and colleagues now help to define the code that permits recognition of phosphotyrosine residues by SH2 domains, the most abundant class of phosphotyrosine binding domains.
    Original languageEnglish
    JournalCell Reports
    Issue number4
    Pages (from-to)1293-1305
    Publication statusPublished - 2013

    Bibliographical note

    This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original author and source are credited.

    This work was supported by the EU FP6 Interaction Proteome integrated project, the FP7 Affinomics project, and the Italian Foundation for Cancer Research (AIRC). M.T. was supported by a donation by
    Cesira Perazzi. Work at C.P.R.’s lab is supported by a grant from the Novo Nordisk Foundation


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