scholarly journals In situ structural analysis of the human nuclear pore complex

Nature ◽  
2015 ◽  
Vol 526 (7571) ◽  
pp. 140-143 ◽  
Author(s):  
Alexander von Appen ◽  
Jan Kosinski ◽  
Lenore Sparks ◽  
Alessandro Ori ◽  
Amanda L. DiGuilio ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Nuclear Pore Complex ◽  
Nuclear Pore

scholarly journals Proteasomes tether to two distinct sites at the nuclear pore complex

2017 ◽  
Vol 114 (52) ◽  
pp. 13726-13731 ◽  
Author(s):  
Sahradha Albert ◽  
Miroslava Schaffer ◽  
Florian Beck ◽  
Shyamal Mosalaganti ◽  
Shoh Asano ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Binding Sites ◽  
Electron Tomography ◽  
Nuclear Pore ◽  
Cellular Environment ◽  
Subtomogram Averaging ◽  
Substrate Processing ◽  
Cellular Components ◽  
Transport Of Macromolecules

The partitioning of cellular components between the nucleus and cytoplasm is the defining feature of eukaryotic life. The nuclear pore complex (NPC) selectively gates the transport of macromolecules between these compartments, but it is unknown whether surveillance mechanisms exist to reinforce this function. By leveraging in situ cryo-electron tomography to image the native cellular environment of Chlamydomonas reinhardtii, we observed that nuclear 26S proteasomes crowd around NPCs. Through a combination of subtomogram averaging and nanometer-precision localization, we identified two classes of proteasomes tethered via their Rpn9 subunits to two specific NPC locations: binding sites on the NPC basket that reflect its eightfold symmetry and more abundant binding sites at the inner nuclear membrane that encircle the NPC. These basket-tethered and membrane-tethered proteasomes, which have similar substrate-processing state frequencies as proteasomes elsewhere in the cell, are ideally positioned to regulate transcription and perform quality control of both soluble and membrane proteins transiting the NPC.

scholarly journals Isolation of the yeast nuclear pore complex.

1993 ◽  
Vol 123 (4) ◽  
pp. 771-783 ◽  
Author(s):  
M P Rout ◽  
G Blobel
Keyword(s):  
Electron Microscopy ◽  
Image Reconstruction ◽  
Nuclear Pore Complex ◽  
Sedimentation Coefficient ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Negative Stain ◽  
Negative Stain Electron Microscopy ◽  
Pore Complexes

Nuclear pore complexes (NPCs) have been isolated from the yeast Saccharomyces. Negative stain electron microscopy of the isolated NPCs and subsequent image reconstruction revealed the octagonal symmetry and many of the ultrastructural features characteristic of vertebrate NPCs. The overall dimensions of the yeast NPC, both in its isolated form as well as in situ, are smaller than its vertebrate counterpart. However, the diameter of the central structures are similar. The isolated yeast NPC has a sedimentation coefficient of approximately 310 S and an M(r) of approximately 66 MD. It retains all but one of the eight known NPC proteins. In addition it contains as many as 80 uncharacterized proteins that are candidate NPC proteins.

scholarly journals In situ architecture of the algal nuclear pore complex

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Shyamal Mosalaganti ◽  
Jan Kosinski ◽  
Sahradha Albert ◽  
Miroslava Schaffer ◽  
Daniela Strenkert ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore

scholarly journals Conformational Changes of the in Situ Nuclear Pore Complex

1999 ◽  
Vol 77 (1) ◽  
pp. 241-247 ◽  
Author(s):  
Hongwei Wang ◽  
David E. Clapham
Keyword(s):  
Conformational Changes ◽  
Nuclear Pore Complex ◽  
Nuclear Pore

Structural analysis of the nuclear pore complex by integrated approaches

2009 ◽  
Vol 19 (2) ◽  
pp. 226-232 ◽  
Author(s):  
Nadav Elad ◽  
Tal Maimon ◽  
Daphna Frenkiel-Krispin ◽  
Roderick YH Lim ◽  
Ohad Medalia
Keyword(s):  
Structural Analysis ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Integrated Approaches

scholarly journals Molecular and structural analysis of central transport channel in complex with Nup93 of nuclear pore complex

2020 ◽  
Vol 29 (12) ◽  
pp. 2510-2527
Author(s):  
Parshuram J. Sonawane ◽  
Pravin Dewangan ◽  
Pankaj Kumar Madheshiya ◽  
Kriti Chopra ◽  
Mohit Kumar ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Transport Channel

scholarly journals Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study

2016 ◽  
Vol 27 (25) ◽  
pp. 3964-3971 ◽  
Author(s):  
Ethan Laudermilch ◽  
Pei-Ling Tsai ◽  
Morven Graham ◽  
Elizabeth Turner ◽  
Chenguang Zhao ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Structural Analysis ◽  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Compositional Analysis ◽  
Immunogold Labeling ◽  
Nuclear Pore ◽  
Functional Link ◽  
Experimental Platform ◽  
Bleb Formation

The human genome encodes four Torsin ATPases, the functions of which are poorly understood. In this study, we use CRISPR/Cas9 engineering to delete all four Torsin ATPases individually and in combination. Using nuclear envelope (NE) blebbing as a phenotypic measure, we establish a direct correlation between the number of inactivated Torsin alleles and the occurrence of omega-shaped herniations within the lumen of the NE. A similar, although not identical, redundancy is observed for LAP1 and LULL1, which serve as regulatory cofactors for a subset of Torsin ATPases. Unexpectedly, deletion of Tor2A in a TorA/B/3A-deficient background results in a stark increase of bleb formation, even though Tor2A does not respond to LAP1/LULL1 stimulation. The robustness of the observed phenotype in Torsin-deficient cells enables a structural analysis via electron microscopy tomography and a compositional analysis via immunogold labeling. Ubiquitin and nucleoporins were identified as distinctively localizing components of the omega-shaped bleb structure. These findings suggest a functional link between the Torsin/cofactor system and NE/nuclear pore complex biogenesis or homeostasis and establish a Torsin-deficient cell line as a valuable experimental platform with which to decipher Torsin function.

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