title: Selectivity and promiscuity in the interaction network mediated by protein recognition modules.
abstract: 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.
authors.affiliation: Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, 00133 Rome, Italy.
authors.forename: Luisa
authors.initials: L
authors.lastname: Castagnoli
authors.forename: Anna
authors.initials: A
authors.lastname: Costantini
authors.forename: Claudia
authors.initials: C
authors.lastname: Dall'Armi
authors.forename: Stefania
authors.initials: S
authors.lastname: Gonfloni
authors.forename: Luisa
authors.initials: L
authors.lastname: Montecchi-Palazzi
authors.forename: Simona
authors.initials: S
authors.lastname: Panni
authors.forename: Serena
authors.initials: S
authors.lastname: Paoluzi
authors.forename: Elena
authors.initials: E
authors.lastname: Santonico
authors.forename: Gianni
authors.initials: G
authors.lastname: Cesareni
mesh_terms: D000818:Animals; D006801:Humans; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D020543:Proteome / Q000737:chemistry; D015398:Signal Transduction; D013379:Substrate Specificity; D020798:Two-Hybrid System Techniques; D018909:src Homology Domains
chemical_list: D010455:Peptides; D011506:Proteins; D020543:Proteome