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

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

Author information

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.

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.

PMID:
26051542
DOI:
10.1016/j.devcel.2015.04.027
[Indexed for MEDLINE]
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