Insulin signaling and the control of PHAS-I phosphorylation.

摘要: The rate of mRNA translation is determined by many factors including a family proteins that control the availability cap-binding protein, eIF4E. prototypic member this was originally described as protein became phosphorylated when rat adipocytes were exposed to insulin (Belsham and Denton 1980), finding presaged important role phosphorylation in controlling protein’s function. had unusual properties remaining solution boiled or acid it named PHAS-I (phosphorylated heat- acid-stable) after its cDNA found lack homology with any others encoding known (Hu et al. 1994). Subsequently, be an eIF4E-binding 4E-BP1 (Pause We have retained earlier nomenclature will refer PHAS proteins. Mammals lower organisms slime mold, insects, fish, birds express one more members (Fig. 1A). not been plants yeast, although latter contain possibly serves homologous function but which has no amino sequence identity proteins, except eIF4E binding domain (Zanchin McCarthy 1995). Thus, distribution nature appears less widespread than eIF4E, probably expressed all eukaryotic organisms. Nevertheless, mammals other species, are mediators actions insulin, growth nutrients on synthesis.