title: The conserved Nup107-160 complex is critical for nuclear pore complex assembly.
abstract: Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes, the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate a function for the conserved Nup107-160 complex in this process. Partial in vivo depletion of Nup133 or Nup107 via RNAi in HeLa cells resulted in reduced levels of multiple nucleoporins and decreased NPC density in the NE. Immunodepletion of the entire Nup107-160 complex from in vitro nuclear assembly reactions produced nuclei with a continuous NE but no NPCs. This phenotype was reversible only if Nup107-160 complex was readded before closed NE formation. Depletion also prevented association of FG-repeat nucleoporins with chromatin. We propose a stepwise model in which postmitotic NPC assembly initiates on chromatin via early recruitment of the Nup107-160 complex.
authors.affiliation: EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
authors.forename: Tobias C
authors.initials: TC
authors.lastname: Walther
authors.forename: Annabelle
authors.initials: A
authors.lastname: Alves
authors.forename: Helen
authors.initials: H
authors.lastname: Pickersgill
authors.forename: Isabelle
authors.initials: I
authors.lastname: Loïodice
authors.forename: Martin
authors.initials: M
authors.lastname: Hetzer
authors.forename: Vincent
authors.initials: V
authors.lastname: Galy
authors.forename: Bastian B
authors.initials: BB
authors.lastname: Hülsmann
authors.forename: Thomas
authors.initials: T
authors.lastname: Köcher
authors.forename: Matthias
authors.initials: M
authors.lastname: Wilm
authors.forename: Terry
authors.initials: T
authors.lastname: Allen
authors.forename: Iain W
authors.initials: IW
authors.lastname: Mattaj
authors.forename: Valérie
authors.initials: V
authors.lastname: Doye
mesh_terms: D000818:Animals; D002457:Cell Extracts; D002614:Chelating Agents / Q000494:pharmacology; D002843:Chromatin / Q000235:genetics / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism* / Q000648:ultrastructure; D005260:Female; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D015778:Minor Histocompatibility Antigens; D009685:Nuclear Envelope / Q000378:metabolism* / Q000648:ultrastructure; D022022:Nuclear Pore / Q000378:metabolism* / Q000648:ultrastructure; D028861:Nuclear Pore Complex Proteins / Q000172:deficiency* / Q000235:genetics; D009687:Nuclear Proteins; D009865:Oocytes; D010641:Phenotype; D029867:Xenopus Proteins; D014982:Xenopus laevis
chemical_list: D002457:Cell Extracts; D002614:Chelating Agents; D002843:Chromatin; D015778:Minor Histocompatibility Antigens; C512772:NUP107 protein, human; C440250:NUP133 protein, human; C440251:NUP160 protein, human; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; C499080:Nup160 protein, Xenopus; D029867:Xenopus Proteins