title: The role of protein disorder in the 14-3-3 interaction network.
abstract: Disordered regions are segments of a protein that do not fold completely and thus remain flexible. These regions have key physiological roles, particularly in phospho-proteins, which are enriched in disorder-promoting residues surrounding their phosphorylation sites. 14-3-3 proteins are ordered hubs that interact with multiple and diverse intrinsically disordered phosphorylated targets. This provides 14-3-3 with the ability to participate in and to regulate multiple signalling networks. Here, I review the effect of structural disorder on the mechanism involved in 14-3-3 protein-protein interactions and how 14-3-3 impacts cell biology through disordered ligands. How 14-3-3 proteins constitute an advantageous system to identify novel classes of biological tools is discussed with a special emphasis on a particular-and innovative-use of small molecules to stabilize 14-3-3 protein complexes, useful to study gene expression, cancer signalling and neurodegenerative diseases.
authors.affiliation: Instituto Tecnológico de Chascomús (IIB-INTECH, CONICET-UNSAM), Chascomús, Argentina. dbustos@intech.gov.ar
authors.forename: Diego M
authors.initials: DM
authors.lastname: Bustos
mesh_terms: D048948:14-3-3 Proteins / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D006801:Humans; D011485:Protein Binding; D017510:Protein Folding; D060066:Protein Interaction Maps; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism
chemical_list: D048948:14-3-3 Proteins; D020033:Protein Isoforms; D014157:Transcription Factors