title: Functional insights from studies on the structure of the nuclear pore and coat protein complexes.
abstract: The nuclear envelope (NE) is a specific extension of the endoplasmic reticulum (ER) that wraps around the nucleus and enables the spatial separation of gene transcription and protein translation, one of the signature features of eukaryotes. Rather than being completely closed, the double lipid bilayer of the NE is perforated at sites where the inner and outer nuclear membranes fuse, resulting in circular openings lined with sharply bent membranes. These openings are filled with nuclear pore complexes (NPCs), enormous protein assemblies that facilitate nuclear transport. The scaffold components of the NPC surprisingly share interesting similarities with elements of coat protein complexes, which have general implications for function and evolution of these membrane-coating complexes. Here I discuss, from a structural perspective, what these findings might teach us.
authors.affiliation: Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. tus@mit.edu
authors.forename: Thomas
authors.initials: T
authors.lastname: Schwartz
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000502:physiology*; D020755:Coat Protein Complex I / Q000737:chemistry / Q000502:physiology*; D008954:Models, Biological; D022022:Nuclear Pore / Q000737:chemistry / Q000502:physiology*; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
chemical_list: D020755:Coat Protein Complex I