title: Folding upon phosphorylation: translational regulation by a disorder-to-order transition.
abstract: 4E binding proteins (4E-BPs) play an important role in the regulation of translation by binding to eukaryotic translation initiation factor 4E (eIF4E) and inhibiting assembly of the eIF4F complex. While phosphorylation of 4E-BPs is known to disrupt their binding to eIF4E, the mechanism by which this occurs has been unclear. In a recent study, Forman-Kay and coworkers demonstrate that this mechanism is primarily structure-based: phosphorylation of 4E-BPs results in a disorder-to-order transition, bringing them from their binding-competent disordered state to a folded state incompatible with eIF4E binding.
authors.affiliation: Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA; Integrated Graduate Program in Physical & Engineering Biology, Yale University, New Haven, CT 06520, USA.
authors.forename: Lauren Ann
authors.initials: LA
authors.lastname: Metskas
authors.affiliation: Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA; Integrated Graduate Program in Physical & Engineering Biology, Yale University, New Haven, CT 06520, USA. Electronic address: elizabeth.rhoades@yale.edu.
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Rhoades
mesh_terms: D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D039561:Eukaryotic Initiation Factor-4E / Q000378:metabolism*; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding
chemical_list: D002352:Carrier Proteins; D039561:Eukaryotic Initiation Factor-4E; D064267:Intrinsically Disordered Proteins
keywords: intrinsically disordered proteins; phosphorylation; translation