Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly

Benjamin Vollmer; Michael Lorenz; Daniel Moreno-Andrés; Mona Bodenhöfer; Paola De Magistris; Susanne Adina Astrinidis; Allana Schooley; Matthias Flötenmeyer; Sebastian Leptihn; Wolfram Antonin

doi:10.1016/j.devcel.2015.04.027

Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly

Dev Cell. 2015 Jun 22;33(6):717-28. doi: 10.1016/j.devcel.2015.04.027. Epub 2015 Jun 4.

Affiliations

¹ Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
² Max Planck Institute for Developmental Biology, Spemannstraße 37, 72076 Tübingen, Germany.
³ Institute for Microbiology and Molecular Biology, University of Hohenheim, Garbenstraße 30, 70599 Stuttgart, Germany.
⁴ Friedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany. Electronic address: wolfram.antonin@tuebingen.mpg.de.

PMID: 26051542
DOI: 10.1016/j.devcel.2015.04.027

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Active Transport, Cell Nucleus
Amino Acid Sequence
Animals
HeLa Cells
Humans
Interphase
Karyopherins / metabolism
Models, Biological
Molecular Sequence Data
Mutagenesis, Site-Directed
Nuclear Envelope / metabolism
Nuclear Pore / metabolism
Nuclear Pore Complex Proteins / chemistry
Nuclear Pore Complex Proteins / genetics
Nuclear Pore Complex Proteins / metabolism*
Nuclear Proteins / metabolism
Protein Interaction Domains and Motifs
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / metabolism
Sequence Homology, Amino Acid
Xenopus Proteins / chemistry
Xenopus Proteins / genetics
Xenopus Proteins / metabolism*
Xenopus laevis
ran GTP-Binding Protein / metabolism

Substances

Karyopherins
NUP107 protein, human
NUP153 protein, human
NUP160 protein, human
Nuclear Pore Complex Proteins
Nuclear Proteins
Nup153 protein, Xenopus
Nup160 protein, Xenopus
Recombinant Proteins
Xenopus Proteins
ran GTP-Binding Protein