title: Juggling key players in NMD initiation.
abstract: In this issue of Structure, Melero and colleagues use electron microscopy combined with biochemistry to provide structural insight into the complex between SMG1, SMG8, SMG9, UPF1, and UPF2, elucidating how key players in nonsense-mediated mRNA decay assemble at the initial steps of the process.
authors.affiliation: Max Planck Institute for Developmental Biology, Spemannstrasse 35, 72076 Tübingen, Germany. Electronic address: fulvia.bono@tuebingen.mpg.de.
authors.forename: Fulvia
authors.initials: F
authors.lastname: Bono
mesh_terms: D004789:Enzyme Activation / Q000502:physiology*; D006801:Humans; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000235:genetics*; D059365:Nonsense Mediated mRNA Decay / Q000502:physiology*; D019869:Phosphatidylinositol 3-Kinases / Q000737:chemistry*; D017346:Protein Serine-Threonine Kinases; D020365:RNA Helicases; D015534:Trans-Activators / Q000737:chemistry*
chemical_list: D046912:Multiprotein Complexes; D019869:Phosphatidylinositol 3-Kinases; D017346:Protein Serine-Threonine Kinases; D020365:RNA Helicases; D015534:Trans-Activators; C514704:SMG1 protein, human; C101828:UPF1 protein, human