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IDPs are common across the three domains of life, being especially abundant in the eukaryotic proteomes. Signaling sequences and sites of posttranslational modifications are located within regions of intrinsic disorder. Disorder-to-order transitions in an IDP are coupled with the adoption of different structures in complexes with different partners. The intrinsic flexibility of IDPs helps different disordered regions to bind to a common binding site on a common partner. This binding diversity plays important roles in both protein-protein interaction networks and likely also in gene regulation networks. Such disorder-based signaling is further modulated in multicellular eukaryotes by alternative splicing, for which splicing events map to regions of disorder much more often than to regions of structure. The combination of disorder and alternative splicing is proposed to provide a mechanism for easily "trying out" different signaling pathways, thereby providing the mechanism for generating signaling diversity and enabling the evolution of cell differentiation and multicellularity. Finally, several small molecules-potential drugs have been shown to act by blocking protein-protein interactions involving intrinsic disorder of one of the partners.