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Selectivity and promiscuity in the interaction network mediated by protein recognition modules
Author(s) -
Castagnoli Luisa,
Costantini Anna,
Dall'Armi Claudia,
Gonfloni Stefania,
Montecchi-Palazzi Luisa,
Panni Simona,
Paoluzi Serena,
Santonico Elena,
Cesareni Gianni
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.03.116
Subject(s) - promiscuity , peptide , protein–protein interaction , computational biology , biology , signal transduction , chemistry , microbiology and biotechnology , biochemistry , ecology
A substantial fraction of protein interactions in the cell is mediated by families of protein modules binding to relatively short linear peptides. Many of these interactions have a high dissociation constant and are therefore suitable for supporting the formation of dynamic complexes that are assembled and disassembled during signal transduction. Extensive work in the past decade has shown that, although member domains within a family have some degree of intrinsic peptide recognition specificity, the derived interaction networks display substantial promiscuity. We review here recent advances in the methods for deriving the portion of the protein network mediated by these domain families and discuss how specific biological outputs could emerge in vivo despite the observed promiscuity in peptide recognition in vitro.