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

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. [Display omitted] •Nup153 binds synthetic membranes via its N terminus•Transportin binding regulates Nup153 synthetic membrane interaction•Nup153 membrane binding is required for interphasic nuclear pore complex assembly•Nup153 recruits the Nup107-160 complex to the inner nuclear membrane Nuclear pore complexes assemble and integrate into the intact nuclear envelope during interphase. Vollmer et al. show that the nucleoporin Nup153 is critical for this process. It binds to the nuclear membrane and recruits the Nup107-160 complex, an essential structural component of nuclear pore complexes, to newly forming pores.