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Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly.
Vollmer, Benjamin; Lorenz, Michael; Moreno-Andrés, Daniel; Bodenhöfer, Mona; De Magistris, Paola; Astrinidis, Susanne Adina; Schooley, Allana; Flötenmeyer, Matthias; Leptihn, Sebastian; Antonin, Wolfram.
Afiliación
  • Vollmer B; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
  • Lorenz M; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
  • Moreno-Andrés D; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
  • Bodenhöfer M; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
  • De Magistris P; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
  • Astrinidis SA; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
  • Schooley A; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
  • Flötenmeyer M; Max Planck Institute for Developmental Biology, Spemannstraße 37, 72076 Tübingen, Germany.
  • Leptihn S; Institute for Microbiology and Molecular Biology, University of Hohenheim, Garbenstraße 30, 70599 Stuttgart, Germany.
  • Antonin W; Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany. Electronic address: wolfram.antonin@tuebingen.mpg.de.
Dev Cell ; 33(6): 717-28, 2015 Jun 22.
Article en En | MEDLINE | ID: mdl-26051542
ABSTRACT
In metazoa, nuclear pore complexes (NPCs) are assembled from constituent nucleoporins by two distinct mechanisms in the re-forming nuclear envelope at the end of mitosis and into the intact nuclear envelope during interphase. Here, we show that the nucleoporin Nup153 is required for NPC assembly during interphase but not during mitotic exit. It functions in interphasic NPC formation by binding directly to the inner nuclear membrane via an N-terminal amphipathic helix. This binding facilitates the recruitment of the Nup107-160 complex, a crucial structural component of the NPC, to assembly sites. Our work further suggests that the nuclear transport receptor transportin and the small GTPase Ran regulate the interaction of Nup153 with the membrane and, in this way, direct pore complex assembly to the nuclear envelope during interphase.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Xenopus / Proteínas de Complejo Poro Nuclear Límite: Animals / Humans Idioma: En Revista: Dev Cell Asunto de la revista: EMBRIOLOGIA Año: 2015 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Xenopus / Proteínas de Complejo Poro Nuclear Límite: Animals / Humans Idioma: En Revista: Dev Cell Asunto de la revista: EMBRIOLOGIA Año: 2015 Tipo del documento: Article País de afiliación: Alemania