PMID:26051542

Citation	Vollmer, B, Lorenz, M, Moreno-Andrés, D, Bodenhöfer, M, De Magistris, P, Astrinidis, SA, Schooley, A, Flötenmeyer, M, Leptihn, S and Antonin, W (2015) Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly. Dev. Cell 33:717-28
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.
Links	PubMed Online version:10.1016/j.devcel.2015.04.027
Keywords	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
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
XENLA:NU153		GO:0031965: nuclear membrane	ECO:0000314:		C		The N-terminal fragment of Xenopus Nup153 fused to EGFP, when ectopically expressed in HeLa cells, localized to the NE, presumably the inner nuclear membrane ( Figures 1F and S1C).	complete CACAO 12838
XENLA:NU153		GO:0051292: nuclear pore complex assembly	ECO:0000315:		P		Organism: Xenopus Laevis Protein: Nup153/Nup153 Figure 3B-D: " Addition of 2 μM importin β, which blocks interphasic NPC assembly (D’Angelo et al., 2006), to nuclei formed under control conditions resulted in a reduction in the number of NPCs per nucleus by approximately 60% when added 50 min after starting the reaction (Figure 3B)."	complete CACAO 12839
XENLA:NU153		GO:0005789: endoplasmic reticulum membrane	ECO:0000315:		C		Orgasnism: Xenopus Laevis Protein: Nup153//Nup153 Figure 6 " Membranes were incubated with control or Nup153-depleted cytosol, re-isolated, and analyzed by western blotting (Figures 6A and 6B ). ... Nup153 depletion severely reduced the quantity of soluble nucleoporins re-isolated with membranes."	complete CACAO 12846
HUMAN:NU153		GO:0016020: membrane	ECO:0000315:		C		To confirm the direct membrane binding of full-length Nup153, we turned to the human ortholog, due to the low expression yield of the Xenopus Nup153. Human Nup153 possesses 42% amino acid identity and 55% similarity with the Xenopus protein. The fluorescently labeled human Nup153 efficiently bound GUVs ( Figure 1G). The corresponding membrane-binding-deficient mutation (V47E in the human protein) abrogated the membrane interaction.	complete CACAO 12811

References

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