The SH2 domain interaction landscape
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The SH2 domain interaction landscape. / Tinti, M.; Kiemer, Lars; Costa, Stefano; Miller, Martin Lee; Sacco, F.; Olsen, Jesper Velgaard; Carducci, M.; Paoluzi, S.; Langone, F.; Workman, Christopher; Blom, Nikolaj; Machida, K.; Thompson, C.M.; Schutkowski, M.; Brunak, Søren; Mann, Matthias; Mayer, B.J.; Castagnoli, L.; Cesareni, G.
In: Cell Reports, Vol. 3, No. 4, 2013, p. 1293-1305.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The SH2 domain interaction landscape
AU - Tinti, M.
AU - Kiemer, Lars
AU - Costa, Stefano
AU - Miller, Martin Lee
AU - Sacco, F.
AU - Olsen, Jesper Velgaard
AU - Carducci, M.
AU - Paoluzi, S.
AU - Langone, F.
AU - Workman, Christopher
AU - Blom, Nikolaj
AU - Machida, K.
AU - Thompson, C.M.
AU - Schutkowski, M.
AU - Brunak, Søren
AU - Mann, Matthias
AU - Mayer, B.J.
AU - Castagnoli, L.
AU - Cesareni, G.
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84876957035&partnerID=8YFLogxK
U2 - 10.1016/j.celrep.2013.03.001
DO - 10.1016/j.celrep.2013.03.001
M3 - Journal article
C2 - 23545499
AN - SCOPUS:84876957035
VL - 3
SP - 1293
EP - 1305
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 4
ER -
ID: 46440109