Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold

Gaik, Monika; Flemming, Dirk; Appen, Alexander von; Kastritis, Panagiotis L.; Mücke, Norbert; Fischer, Jessica; Stelter, Philipp; Ori, Alessandro; Bui, Khanh Huy; Baßler, Jochen; Barbar, Elisar; Beck, Martin; Hurt, Ed

doi:10.1083/jcb.201411003

Cited by 69 publications

(106 citation statements)

References 78 publications

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“…2). Nup82, Nup159, together with a pool of Nsp1 that is separate from the central Nsp1-Nup57-Nup49 complex, form a trimeric 1:1:1 complex at the base of the filaments [48,83]. The three proteins are likely held together by an interaction between their C-terminal coiled-coil regions.…”

Section: Components Of the Cytoplasmic Sidementioning

confidence: 99%

The Structure Inventory of the Nuclear Pore Complex

Schwartz

2016

Journal of Molecular Biology

100

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The nuclear pore complex is the principal gateway for molecular exchange between nucleus and cytoplasm across the nuclear envelope. Due to its sheer size of estimated 50–112 MDa and its complex buildup from about 500–1000 individual proteins, it is a difficult object to study for structural biologists. Here I review the extensive ensemble of high-resolution structures of the building blocks of the NPC. Concurrent with the increase in size and complexity, these latest, large structures and assemblies can now be used as the basis for hybrid approaches, primarily in combination with cryo-electron microscopic analysis, generating the first structure-based assembly models of the NPC. Going forward, the structures will be critically important for a detailed analysis of the NPC, including function, evolution, and assembly.

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Section: Components Of the Cytoplasmic Sidementioning

confidence: 99%

The Structure Inventory of the Nuclear Pore Complex

Schwartz

2016

Journal of Molecular Biology

100

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“…Recent structural data for a reconstituted Nup82 module suggest that the C-terminal portion of Nup159, which includes the DID and the C-terminal helices, forms the structural backbone of the complex, along which the other subunits – Nup82, Nsp1, and Dyn2 – become organized, and that this segment of Nup159 is required for organization of the whole complex [105]. Critical to this process is a short, weakly predicted coiled-coil sequence separated from the DID domain by a flexible linker, and shown in vivo to be essential for NPC assembly [98].…”

Section: Lc8 Cross-linking Of Idp Duplex Scaffoldsmentioning

confidence: 99%

Multivalent IDP assemblies: Unique properties of LC8‐associated, IDP duplex scaffolds

et al. 2015

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A wide variety of subcellular complexes are composed of one or more intrinsically disordered proteins (IDPs) that are multivalent, flexible, and characterized by dynamic binding of diverse partner proteins. These multivalent IDP assemblies, of broad functional diversity, are classified here into five categories distinguished by the number of IDP chains and the arrangement of partner proteins in the functional complex. Examples of each category are summarized in the context of the exceptional molecular and biological properties of IDPs. One type – IDP duplex scaffolds – is considered in detail. Its unique features include parallel alignment of two IDP chains, formation of new self-associated domains, enhanced affinity for additional bivalent ligands, and ubiquitous binding of the hub protein LC8. For two IDP duplex scaffolds, dynein intermediate chain IC and nucleoporin Nup159, these duplex features, together with the inherent flexibility of IDPs, are central to their assembly and function. A new type of IDP-LC8 interaction, distributed binding of LC8 among multiple IDP recognition sites, is described for Nup159 assembly.

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“…The core of the Nup82 complex is composed of the proteins Nup82, Nup159, and Nsp1. Fragments of each have been solved crystallographically (Chug et al, 2015; Stuwe et al, 2015a; Yoshida et al, 2011), and negative stain EM revealed this complex to have an overall “P-shaped” morphology (Gaik et al, 2015), but no structures exist for either the whole complex or how it interacts with its associated proteins and the NPC.…”

Section: Introductionmentioning

confidence: 99%

Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform

Fernández-Martı́nez

Kim

Shi

et al. 2016

Cell

151

218

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Summary The last steps in mRNA export and remodeling are performed by the Nup82 complex, a large conserved assembly at the cytoplasmic face of the nuclear pore complex (NPC). By integrating diverse structural data, we have determined the molecular architecture of the native Nup82 complex at subnanometer precision. The complex consists of two compositionally identical multiprotein subunits that adopt different configurations. The Nup82 complex fits into the NPC through the outer ring Nup84 complex. Our map shows that this entire 14 MDa Nup82-Nup84 complex assembly positions the cytoplasmic mRNA export factor docking sites and mRNP remodeling machinery right over the NPC's central channel, rather than on distal cytoplasmic filaments as previously supposed. We suggest that this configuration efficiently captures and remodels exporting mRNP particles immediately upon reaching the cytoplasmic side of the NPC.

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Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold

Abstract: The yeast Nup82 complex forms an unusual asymmetric structure with a dimeric array of subunits that mediate its anchorage to the NPC scaffold and its concomitant interaction with the soluble nucleocytoplasmic transport machinery.

Cited by 69 publications

References 78 publications

The Structure Inventory of the Nuclear Pore Complex

The Structure Inventory of the Nuclear Pore Complex

Multivalent IDP assemblies: Unique properties of LC8‐associated, IDP duplex scaffolds

Structure and Function of the Nuclear Pore Complex Cytoplasmic mRNA Export Platform

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