Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly

Vollmer, Benjamin; Schooley, Allana; Sachdev, Ruchika; Eisenhardt, Nathalie; Schneider, A.M.; Sieverding, Cornelia; Madlung, Johannes; Gerken, Uwe; Maček, Boris; Antonin, Wolfram

doi:10.1038/emboj.2012.256

Cited by 110 publications

(157 citation statements)

References 63 publications

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“…5D). The inner ring is anchored to the pore membrane through membrane-binding motifs (MBMs) on the β-propellers at the N-termini of Nup157 and Nup170, and on the C-termini of Nup53 and Nup59 17–19 . These proteins also interact with the scaffold-facing domains of Pom152, Ndc1, and Pom34, each of which carry transmembrane domains (TMDs) (Fig.…”

Section: Resultsmentioning

confidence: 99%

Integrative structure and functional anatomy of a nuclear pore complex

Kim

Fernández-Martı́nez

Nudelman

et al. 2018

Nature

490

894

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Summary Despite the central role of Nuclear Pore Complexes (NPCs) as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm, their large size and dynamic nature have impeded a full structural and functional elucidation. Here, we have determined a subnanometer precision structure for the entire 552-protein yeast NPC by satisfying diverse data including stoichiometry, a cryo-electron tomography map, and chemical cross-links. The structure reveals the NPC’s functional elements in unprecedented detail. The NPC is built of sturdy diagonal columns to which are attached connector cables, imbuing both strength and flexibility, while tying together all other elements of the NPC, including membrane-interacting regions and RNA processing platforms. Inwardly-directed anchors create a high density of transport factor-docking Phe-Gly repeats in the central channel, organized in distinct functional units. Taken together, this integrative structure allows us to rationalize the architecture, transport mechanism, and evolutionary origins of the NPC.

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Section: Resultsmentioning

confidence: 99%

Integrative structure and functional anatomy of a nuclear pore complex

Kim

Fernández-Martı́nez

Nudelman

et al. 2018

Nature

490

894

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“…NDC1 is also likely to be involved at this step (Mansfeld et al, 2006;Stavru et al, 2006) but its function is less defined. Components of the second major structural subunit of the NPC, the Nup93 complex, subsequently assemble stepwise from the membrane building laterally towards the centre of the NPC (Dultz et al, 2008;Sachdev et al, 2012;Vollmer et al, 2012), which allows for the recruitment of the central channel components, the FGnucleoporins. The final steps of NPC assembly are the addition of peripheral nucleoporins, which form extensions to the cytoplasmic and nucleoplasmic sides of the pore (Bodoor et al, 1999;Hase and Cordes, 2003;Dultz et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

The lysine demethylase LSD1 is required for nuclear envelope formation at the end of mitosis

Schooley

Moreno-Andrés

Magistris

et al. 2015

Journal of Cell Science

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The metazoan nucleus breaks down and reassembles during each cell division. Upon mitotic exit, the successful reestablishment of an interphase nucleus requires the coordinated reorganization of chromatin and formation of a functional nuclear envelope. Here, we report that the histone demethylase LSD1 (also known as KDM1A) plays a crucial role in nuclear assembly at the end of mitosis. Downregulation of LSD1 in cells extends telophase and impairs nuclear pore complex assembly. In vitro, LSD1 demethylase activity is required for the recruitment of MEL28 (also known as ELYS and AHCTF1) and nuclear envelope precursor vesicles to chromatin, crucial steps in nuclear reassembly. Accordingly, the formation of a closed nuclear envelope and nuclear pore complex assembly are impaired upon depletion of LSD1 or inhibition of its activity. Our results identify histone demethylation by LSD1 as a new regulatory mechanism linking the chromatin state and nuclear envelope formation at the end of mitosis.

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“…Other nucleoporins, such as Nup53 and Nup155 are also involved in NPC assembly into the nuclear envelope. Nup53, for instance, directly interacts with the nuclear envelope both in yeast and Xenopus (Marelli et al, 2001;Vollmer et al, 2012). In addition, several studies have identified interactions between Nup53 and transmembrane protein Ndc1 (Mansfeld et al, 2006;Onischenko et al, 2009;Eisenhardt et al, 2014;HawrylukGara et al, 2008).…”

Section: Roles Of Npcs and Linc Complexes In Nuclear Envelope Architementioning

confidence: 99%

The LINC and NPC relationship – it's complicated!

Jahed

Soheilypour

Peyro

et al. 2016

Journal of Cell Science

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The genetic information of eukaryotic cells is enclosed within a double-layered nuclear envelope, which comprises an inner and outer nuclear membrane. Several transmembrane proteins locate to the nuclear envelope; however, only two integral protein complexes span the nuclear envelope and connect the inside of the nucleus to the cytoplasm. The nuclear pore complex (NPC) acts as a gateway for molecular exchange between the interior of the nucleus and the cytoplasm, whereas so-called LINC complexes physically link the nucleoskeleton and the cytoskeleton. In this Commentary, we will discuss recent studies that have established direct functional associations between these two complexes. The assembly of NPCs and their even distribution throughout the nuclear envelope is dependent on components of the LINC complex. Additionally, LINC complex formation is dependent on the successful localization of inner nuclear membrane components of LINC complexes and their transport through the NPC. Furthermore, the architecture of the nuclear envelope depends on both protein complexes. Finally, we will present recent evidence showing that LINC complexes can affect nucleo-cytoplasmic transport through the NPC, further highlighting the importance of understanding the associations of these essential complexes at the nuclear envelope.

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Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly

Abstract: Nuclear pore formation depends on membrane curvature. The membrane deforming activity of Nup53 is required for nuclear pore complex (NPC) assembly during interphase.

Cited by 110 publications

References 63 publications

Integrative structure and functional anatomy of a nuclear pore complex

Integrative structure and functional anatomy of a nuclear pore complex

The lysine demethylase LSD1 is required for nuclear envelope formation at the end of mitosis

The LINC and NPC relationship – it's complicated!

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