Selectivity and promiscuity in the interaction network mediated by protein recognition modules
详细信息 查看全文
- 作者：Castagnoli ; Luisa ; Costantini ; Anna ; Dall'Armi ; Claudia ; Gonfloni ; Stefania ; Montecchi-Palazzi ; Luisa ; et. al.
- 关键词：SH3 ; src homology 3 ; SH2 ; src homology 2 ; WISE ; whole interactome scanning experiment ; Protein interaction ; SH3 ; Protein domains ; Interaction networks
- 刊名：FEBS Letters
- 出版年：2004
- 出版时间：June 1, 2004
- 年：2004
- 卷：567
- 期：1
- 页码：74-79
- 全文大小：193 K
文摘
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.