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.

Castagnoli, L., Costantini, A., Dall'Armi, C., Gonfloni, S., Montecchi Palazzi, L., Panni, S., et al. (2004). Selectivity and promiscuity in the interaction network mediated by protein recognition modules. FEBS LETTERS, 567(1), 74-79 [10.1016/j.febslet.2004.03.116].

Selectivity and promiscuity in the interaction network mediated by protein recognition modules

CASTAGNOLI, LUISA;GONFLONI, STEFANIA;PAOLUZI, SERENA;SANTONICO, ELENA;CESARENI, GIOVANNI
2004-06-01

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.
1-giu-2004
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/18 - GENETICA
English
Animals; Humans; Two-Hybrid System Techniques; Proteome; Proteins; Peptides; Substrate Specificity; Protein Structure, Tertiary; Protein Binding; Signal Transduction; src Homology Domains; Protein Conformation
Castagnoli, L., Costantini, A., Dall'Armi, C., Gonfloni, S., Montecchi Palazzi, L., Panni, S., et al. (2004). Selectivity and promiscuity in the interaction network mediated by protein recognition modules. FEBS LETTERS, 567(1), 74-79 [10.1016/j.febslet.2004.03.116].
Castagnoli, L; Costantini, A; Dall'Armi, C; Gonfloni, S; Montecchi Palazzi, L; Panni, S; Paoluzi, S; Santonico, E; Cesareni, G
Articolo su rivista
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/96338
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