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Peptide microarrays for the detection of molecular interactions in cellular signal transduction
Author(s) -
Stoevesandt Oda,
Elbs Martin,
Köhler Karsten,
Lellouch Annemarie C.,
Fischer Rainer,
André Thomas,
Brock Roland
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200401095
Subject(s) - signal transduction , protein array analysis , peptide , sh2 domain , dna microarray , biology , microbiology and biotechnology , protein–protein interaction , transduction (biophysics) , cell signaling , tyrosine kinase , computational biology , chemistry , biochemistry , gene expression , gene
The formation of protein complexes is a hallmark of cellular signal transduction. Here, we show that peptide microarrays provide a robust and quantitative means to detect signalling‐dependent changes of molecular interactions. Recruitment of a protein into a complex upon stimulation of a cell leads to the masking of an otherwise exposed binding site. In cell lysates this masking can be detected by reduced binding to a microarray carrying a peptide that corresponds to the binding motif of the respective interaction domain. The method is exemplified for the lymphocyte‐specific tyrosine kinase 70 kDa zeta‐associated protein binding to a bis‐phosphotyrosine‐motif of the activated T‐cell receptor via its tandem SH2 domain. Compared to established techniques, the method provides a significant shortcut to the detection of molecular interactions.