Nuclear pore complex components have temperature‐influenced roles in plant growth and immunity

2020 ◽  
Vol 43 (6) ◽  
pp. 1452-1466 ◽  
Author(s):  
Aiqin Zhang ◽  
Shuai Wang ◽  
Jitae Kim ◽  
Jiapei Yan ◽  
Xiufeng Yan ◽  
...  
Keyword(s):  
Plant Growth ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Components

scholarly journals Nuclear Pore Complex Components in the Malaria Parasite Plasmodium berghei

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Jessica Kehrer ◽  
Claudia Kuss ◽  
Amparo Andres-Pons ◽  
Anna Reustle ◽  
Noa Dahan ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Plasmodium Berghei ◽  
Malaria Parasite ◽  
Nuclear Pore ◽  
Parasite Plasmodium ◽  
Complex Components

scholarly journals Identification and Characterization of Nuclear Pore Complex Components in Arabidopsis thaliana

2010 ◽  
Vol 22 (12) ◽  
pp. 4084-4097 ◽  
Author(s):  
Kentaro Tamura ◽  
Yoichiro Fukao ◽  
Masaaki Iwamoto ◽  
Tokuko Haraguchi ◽  
Ikuko Hara-Nishimura
Keyword(s):  
Arabidopsis Thaliana ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Identification And Characterization ◽  
Complex Components

scholarly journals Characterization of nuclear pore complex components in fission yeastSchizosaccharomyces pombe

Nucleus ◽  
2014 ◽  
Vol 5 (2) ◽  
pp. 149-162 ◽  
Author(s):  
Haruhiko Asakawa ◽  
Hui-Ju Yang ◽  
Takaharu G Yamamoto ◽  
Chizuru Ohtsuki ◽  
Yuji Chikashige ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Complex Components

The Formation, Structure, Distribution and Frequency of Nuclear Pores

1971 ◽  
Vol 29 ◽  
pp. 518-519
Author(s):  
G. G. Maul
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Membrane ◽  
Dynamic Structure ◽  
Nuclear Pore ◽  
Nuclear Pores ◽  
Filter Function ◽  
Etching Technique ◽  
Selective Filter ◽  
Membranous Part

The chromatin of eukaryotic cells is separated from the cytoplasm by a double membrane. One obvious structural specialization of the nuclear membrane is the presence of pores which have been implicated to facilitate the selective nucleocytoplasmic exchange of a variety of large molecules. Thus, the function of nuclear pores has mainly been regarded to be a passive one. Non-membranous diaphragms, radiating fibers, central rings, and other pore-associated structures were thought to play a role in the selective filter function of the nuclear pore complex. Evidence will be presented that suggests that the nuclear pore is a dynamic structure which is non-randomly distributed and can be formed during interphase, and that a close relationship exists between chromatin and the membranous part of the nuclear pore complex.Octagonality of the nuclear pore complex has been confirmed by a variety of techniques. Using the freeze-etching technique, it was possible to show that the membranous part of the pore complex has an eight-sided outline in human melanoma cells in vitro. Fibers which traverse the pore proper at its corners are continuous and indistinguishable from chromatin at the nucleoplasmic side, as seen in conventionally fixed and sectioned material. Chromatin can be seen in octagonal outline if serial sections are analyzed which are parallel but do not include nuclear membranes (Fig. 1). It is concluded that the shape of the pore rim is due to fibrous material traversing the pore, and may not have any functional significance. In many pores one can recognize a central ring with eight fibers radiating to the corners of the pore rim. Such a structural arrangement is also found to connect eight ribosomes at the nuclear membrane.

Structure, assembly and interactions of the nuclear lamina and the nuclear pore complex

1992 ◽  
Vol 50 (1) ◽  
pp. 490-491
Author(s):  
N. Panté ◽  
M. Jarnik ◽  
E. Heitlinger ◽  
U. Aebi
Keyword(s):  
Nuclear Pore Complex ◽  
Divalent Cations ◽  
Nuclear Lamina ◽  
Dynamic Structure ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Pore ◽  
Cytoplasmic Filaments ◽  
Radial Spokes ◽  
Nuclear Ring ◽  
Central Plug

The nuclear pore complex (NPC) is a ∼120 MD supramolecular machine implicated in nucleocytoplasmic transport, that is embedded in the double-membraned nuclear envelope (NE). The basic framework of the ∼120 nm diameter NPC consists of a 32 MD cytoplasmic ring, a 66 MD ‘plug-spoke’ assembly, and a 21 MD nuclear ring. The ‘central plug’ seen in en face views of the NPC reveals a rather variable appearance indicating that it is a dynamic structure. Projecting from the cytoplasmic ring are 8 short, twisted filaments (Fig. 1a), whereas the nuclear ring is topped with a ‘fishtrap’ made of 8 thin filaments that join distally to form a fragile, 30-50 nm distal diameter ring centered above the NPC proper (Fig. 1b). While the cytoplasmic filaments are sensitive to proteases, they as well as the nuclear fishtraps are resistant to RNase treatment. Removal of divalent cations destabilizes the distal rings and thereby opens the fishtraps, addition causes them to reform. Protruding from the tips of the radial spokes into perinuclear space are ‘knobs’ that might represent the large lumenal domain of gp210, a membrane-spanning glycoprotein (Fig. 1c) which, in turn, may play a topogenic role in membrane folding and/or act as a membrane-anchoring site for the NPC. The lectin wheat germ agglutinin (WGA) which is known to recognize the ‘nucleoporins’, a family of glycoproteins having O-linked N-acetyl-glucosamine, is found in two locations on the NPC (Fig. 1. d-f): (i) whereas the cytoplasmic filaments appear unlabelled (Fig. 1d&e), WGA-gold labels sites between the central plug and the cytoplasmic ring (Fig. le; i.e., at a radius of 25-35 nm), and (ii) it decorates the distal ring of the nuclear fishtraps (Fig. 1, d&f; arrowheads).

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