The SH2 domain interaction landscape

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 - 2013/4/25

Y1 - 2013/4/25

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

SN - 2639-1856

VL - 3

SP - 1293

EP - 1305

JO - Cell Reports

JF - Cell Reports

IS - 4

ER -