Correction: Components of Coated Vesicles and Nuclear Pore Complexes Share a Common Molecular Architecture

Nuclear pore complexes (NPCs) are large macromolecular machines that mediate the traffic between the nucleus and the cytoplasm. In vertebrates, each NPC consists of ∼1000 proteins, termed nucleoporins, and has a mass of over 100 MDa. While a pseudo-atomic static model of the central scaffold of the NPC has recently been assembled by integrating data from isolated proteins and complexes, many structural components still remain elusive due to the enormous size and flexibility of the NPC. Here, we explored the power of 3D super-resolution microscopy combined with computational classification and averaging to explore the 3D structure of the NPC in single human cells. We show that this approach can build the first integrated 3D structural map containing both central as well as peripheral NPC subunits with molecular specificity and nanoscale resolution. Our unbiased classification of over ten thousand individual NPCs indicates that the nuclear ring and the nuclear basket can adopt different conformations. Our approach opens up the exciting possibility to relate different structural states of the NPC to function in situ.

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Nuclear Pore Transport: Insight in Situ

Microscopy and Microanalysis ◽

10.1017/s1431927600024909 ◽

1998 ◽

Vol 4 (S2) ◽

pp. 956-957

Author(s):

U. Aebi ◽

D. Stoffler ◽

B. Feja ◽

K. Goldie

Keyword(s):

Nuclear Periphery ◽

3D Structure ◽

Nuclear Pore ◽

Nuclear Pore Complexes ◽

Molecular Architecture ◽

Energy Filtering ◽

3D Architecture ◽

Bidirectional Transport ◽

Pore Complexes

The nuclear envelope (NE) physically separates the genetic machinery residing in the nucleus from protein synthesis taking place in the cytoplasm. Bidirectional transport of proteins, RNAs and RNP particles between these two compartments is mediated by the nuclear pore complexes (NPCs), large (-120 MDa) supramolecular assemblies embedded in the NE and being built of -100 different polypeptides, called nucleoporins. Extensive structural studies have revealed the 3D architecture of NPCs, and epitopes of several nucleoporins have been localized within their 3D structure.In an attempt to go beyond the current consensus model of the NPC (Fig. lc, inset), we have embarked on a more systematic structural analysis of the molecular architecture of native NPCs. This is achieved by field-emission (FETEM; Fig. la) or energy-filtering (EFTEM; Fig. lb) TEM of completely unfixed and unstained Xenopus oocyte NEs embedded in thick (i.e. -200 nm) amorphous ice so that the 3D organization of the cytoplasmic and nuclear periphery of the NPCs (i.e. the cytoplasmic fibrils and nuclear baskets) is fully preserved (Fig. lb).

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Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae

The Journal of Cell Biology ◽

10.1083/jcb.201108124 ◽

2012 ◽

Vol 196 (1) ◽

pp. 19-27 ◽

Cited By ~ 35

Author(s):

Akira Hayakawa ◽

Anna Babour ◽

Lucie Sengmanivong ◽

Catherine Dargemont

Keyword(s):

Posttranslational Modifications ◽

Systematic Approach ◽

Protein Transport ◽

Nuclear Pore ◽

Nuclear Pore Complexes ◽

Molecular Architecture ◽

Dynein Light Chain ◽

Large Protein ◽

Pore Complexes ◽

Cytoplasmic Side

Nuclear pore complexes (NPCs) correspond to large protein transport complexes responsible for selective nucleocytoplasmic exchange. Although research has revealed much about the molecular architecture and roles of the NPC subcomplexes, little is known about the regulation of NPC functions by posttranslational modifications. We used a systematic approach to show that more than half of NPC proteins were conjugated to ubiquitin. In particular, Nup159, a nucleoporin exclusively located on the cytoplasmic side of the NPC, was monoubiquitylated by the Cdc34/SCF (Skp1–Cdc53–F-box E3 ligase) enzymes. Preventing this modification had no consequences on nuclear transport or NPC organization but strongly affected the ability of Nup159 to target the dynein light chain to the NPC. This led to defects in nuclear segregation at the onset of mitosis. Thus, defining ubiquitylation of the yeast NPC highlights yet-unexplored functions of this essential organelle in cell division.

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3D super-resolution fluorescence microscopy maps the variable molecular architecture of the Nuclear Pore Complex

10.1101/2020.11.27.386599 ◽

2020 ◽

Author(s):

Vilma Jimenez Sabinina ◽

M. Julius Hossain ◽

Jean-Karim Hériché ◽

Philipp Hoess ◽

Bianca Nijmeijer ◽

...

Keyword(s):

3D Structure ◽

Super Resolution ◽

Nuclear Pore ◽

Nuclear Pore Complexes ◽

Molecular Architecture ◽

Nuclear Ring ◽

Molecular Specificity ◽

Pore Complexes ◽

Super Resolution Microscopy ◽

Exciting Possibility

AbstractNuclear pore complexes (NPCs) are large macromolecular machines that mediate the traffic between the nucleus and the cytoplasm. In vertebrates, each NPC consists of ∼1000 proteins, termed nucleoporins, and has a mass of over 100 MDa. While a pseudo-atomic static model of the central scaffold of the NPC has recently been assembled by integrating data from isolated proteins and complexes, many structural components still remain elusive due to the enormous size and flexibility of the NPC. Here, we explored the power of 3D super-resolution microscopy combined with computational classification and averaging to explore the 3D structure of the NPC in single human cells. We show that this approach can build the first integrated 3D structural map containing both central as well as peripheral NPC subunits with molecular specificity and nanoscale resolution. Our unbiased classification of over ten thousand individual NPCs indicates that the nuclear ring and the nuclear basket can adopt different conformations. Our approach opens up the exciting possibility to relate different structural states of the NPC to function in situ.

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Nuclear Envelope Dynamics During Mitosis

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100103188 ◽

1988 ◽

Vol 46 ◽

pp. 224-225

Author(s):

Brian Burke

Keyword(s):

Nuclear Envelope ◽

Membrane Vesicles ◽

Nuclear Pore ◽

Nuclear Pore Complexes ◽

Animal Cells ◽

Interphase Chromosome ◽

Lamin B ◽

Chromosome Architecture ◽

Complex Membrane ◽

Pore Complexes

The nuclear envelope is a complex membrane structure that forms the boundary of the nuclear compartment in eukaryotes. It regulates the passage of macromolecules between the two compartments and may be important for organizing interphase chromosome architecture. In interphase animal cells it forms a remarkably stable structure consisting of a double membrane ouerlying a protein meshwork or lamina and penetrated by nuclear pore complexes. The latter form the channels for nucleocytoplasmic exchange of macromolecules, At the onset of mitosis, however, it rapidly disassembles, the membranes fragment to yield small vesicles and the lamina, which is composed of predominantly three polypeptides, lamins R, B and C (MW approx. 74, 68 and 65 kDa respectiuely), breaks down. Lamins B and C are dispersed as monomers throughout the mitotic cytoplasm, while lamin B remains associated with the nuclear membrane vesicles.

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Pore relations: nuclear pore complexes and nucleocytoplasmic exchange

Essays in Biochemistry ◽

10.1042/bse0360075 ◽

2000 ◽

Vol 36 ◽

pp. 75-88 ◽

Cited By ~ 18

Author(s):

Michael P. Rout ◽

John D. Aitchison

Keyword(s):

Nuclear Pore ◽

Nuclear Pore Complexes ◽

Pore Complexes

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