scholarly journals Nanoscale Mechanism of Molecular Transport through the Nuclear Pore Complex As Studied by Scanning Electrochemical Microscopy

2013 ◽  
Vol 135 (6) ◽  
pp. 2321-2329 ◽  
Author(s):  
Jiyeon Kim ◽  
Anahita Izadyar ◽  
Nikoloz Nioradze ◽  
Shigeru Amemiya
Keyword(s):  
Nuclear Pore Complex ◽  
Molecular Transport ◽  
Scanning Electrochemical Microscopy ◽  
Nuclear Pore ◽  
Electrochemical Microscopy

scholarly journals Nanoscale electrostatic gating of molecular transport through nuclear pore complexes as probed by scanning electrochemical microscopy

2019 ◽  
Vol 10 (34) ◽  
pp. 7929-7936
Author(s):  
Pavithra Pathirathna ◽  
Ryan J. Balla ◽  
Guanqun Meng ◽  
Zemeng Wei ◽  
Shigeru Amemiya
Keyword(s):  
Amino Acids ◽  
Nuclear Pore Complex ◽  
Molecular Transport ◽  
Scanning Electrochemical Microscopy ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Electrostatic Gating ◽  
Pore Complexes ◽  
Electrochemical Microscopy

The nuclear pore complex (NPC) uses positive residues of amino acids to electrostatically regulate molecular transport through the peripheral route.

scholarly journals Probing High Permeability of Nuclear Pore Complexes by Scanning Electrochemical Microscopy: Ca2+Effects on Transport Barriers

2019 ◽  
Vol 91 (8) ◽  
pp. 5446-5454 ◽  
Author(s):  
Pavithra Pathirathna ◽  
Ryan J. Balla ◽  
Dylan T. Jantz ◽  
Niraja Kurapati ◽  
Erin R. Gramm ◽  
...  
Keyword(s):  
Scanning Electrochemical Microscopy ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
High Permeability ◽  
Transport Barriers ◽  
Pore Complexes ◽  
Electrochemical Microscopy

scholarly journals Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex

2010 ◽  
Vol 391 (7) ◽  
Author(s):  
Orit Peleg ◽  
Roderick Y.H. Lim
Keyword(s):  
Nuclear Pore Complex ◽  
Intrinsically Disordered Proteins ◽  
Molecular Transport ◽  
Disordered Proteins ◽  
Nuclear Pore ◽  
Biological Mechanisms ◽  
Intrinsically Disordered ◽  
Polymeric Chains ◽  
Insight Into

Abstract Several biological mechanisms involve proteins or proteinaceous components that are intrinsically disordered. A case in point pertains to the nuclear pore complex (NPC), which regulates molecular transport between the nucleus and the cytoplasm. NPC functionality is dependent on unfolded domains rich in Phe-Gly (FG) repeats (i.e., FG-domains) that collectively act to promote or hinder cargo translocation. To a large extent, our understanding of FG-domain behavior is limited to in vitro investigations given the difficulty to resolve them directly in the NPC. Nevertheless, recent findings indicate a collective convergence towards rationalizing FG-domain function. This review aims to glean further insight into this fascinating problem by taking an objective look at the boundary conditions and contextual details underpinning FG-domain behavior in the NPC. Here, we treat the FG-domains as being commensurate with polymeric chains to address ambiguities such as for instance, how FG-domains tethered to the central channel of the NPC would behave differently as compared with their free-floating counterparts in solution. By bringing such fundamental questions to the fore, this review seeks to illuminate the importance of how such parameters can hold influence over the structure-function relation of intrinsically disordered proteins in the NPC and beyond.

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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