tailieunhanh - Báo cáo khoa học: Dynamic interactions of proteins in complex networks: a more structured view

Virtually every process in a cell is carried out by macromolecular com-plexes whose actions need to be perfectly orchestrated. The synchronization and regulation of these biological functions is indeed critical and is usually carried out by complex networks of transient protein interactions. Here, we review some of the many strategies that proteins in regulatory networks use to achieve the dynamic plasticity necessary to rapidly respond to diverse cellular needs. | ễFEBS Journal MINIREVIEW Dynamic interactions of proteins in complex networks a more structured view Amelie Stein1 2 Roland A. Pache1 2 Pau Bernado1 Miquel Pons1 3 and Patrick Aloy1 2 4 1 Institute for Research in Biomedicine Barcelona Spain 2 Barcelona Supercomputing Center Spain 3 Departament de Quimica Organica Universitat de Barcelona Spain 4 Institucio Catalana de Recerca i Estudis Avancats Barcelona Spain Keywords interaction specificity intrinsically unstructured proteins linear motifs modular recognition domains peptide-mediated interactions phosphorylation events post-translationalmodifications protein disorder protein interaction networks signalling networks Correspondence P. Aloy Institute for Research in Biomedicine c Baldiri i Reixac 10-12 08028 Barcelona Spain Fax 34 934 039 954 Tel 34 934 039 690 E-mail These authors contributed equally to this study Received 1 June 2009 revised 18 July 2009 accepted 29 July 2009 Virtually every process in a cell is carried out by macromolecular complexes whose actions need to be perfectly orchestrated. The synchronization and regulation of these biological functions is indeed critical and is usually carried out by complex networks of transient protein interactions. Here we review some of the many strategies that proteins in regulatory networks use to achieve the dynamic plasticity necessary to rapidly respond to diverse cellular needs. More specifically we present recent work on the molecular bases of transient peptide-mediated interactions and the role that post-translational modifications and disordered regions might play. Finally in light of some recent findings we speculate on the possibility of a new regulatory code for intrinsically disordered proteins and the potential biophysical and functional advantages that disorder might provide. doi Introduction Proteins are the main perpetrators of most biological processes. However they seldom act alone .