ArticleProceedings of the National Academy of Sciences of the United States of America1999
Nuclear hourglass technique: an approach that detects electrically open nuclear pores in Xenopus laevis oocyte.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Characterization of Single-Nucleus Electrical Properties by Microfluidic Constriction Channel.Micromachines · 2019Article
- Nuclear pores enable sustained perinuclear calcium oscillations.BMC systems biology · 2016Article
- Towards the Physics of Calcium Signalling in Plants.Plants (Basel, Switzerland) · 2013Review
- Single-molecule transport across an individual biomimetic nuclear pore complex.Nature nanotechnology · 2011Article
- Ion channels at the nucleus: electrophysiology meets the genome.Molecular plant · 2010Review
- Atomic force microscopy visualises a hydrophobic meshwork in the central channel of the nuclear pore.Pflugers Archiv : European journal of physiology · 2008Article
- Towards reconciling structure and function in the nuclear pore complex.Histochemistry and cell biology · 2008Review
- Biology and biophysics of the nuclear pore complex and its components.International review of cell and molecular biology · 2008Review
- Ethanol alters access to the cell nucleus.Pflugers Archiv : European journal of physiology · 2007Article
- Transient permeability leak of nuclear envelope induced by aldosterone.The Journal of membrane biology · 2004Article
- Nuclear envelope: nanoarray responsive to aldosterone.The Journal of membrane biology · 2004Review
- Passive transport of macromolecules through Xenopus laevis nuclear envelope.The Journal of membrane biology · 2003Article
- Intracellular calcium: a prerequisite for aldosterone action.The Journal of membrane biology · 2003Article
- Aldosterone signaling pathway across the nuclear envelope.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Yeast nucleoporins involved in passive nuclear envelope permeability.The Journal of cell biology · 2000Article
- Permeating the nuclear pore complex.Nucleus (Austin, Tex.)Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear pore complexes (NPCs) mediate both active transport and passive diffusion across the nuclear envelope (NE). Determination of NE electrical conductance, however, has been confounded by the lack of an appropriate technical approach. The nuclear patch clamp technique is restricted to preparations with electrically closed NPCs, and microelectrode techniques fail to resolve the extremely low input resistance of large oocyte nuclei. To address the problem, we have developed an approach for measuring the NE electrical conductance of Xenopus laevis oocyte nuclei. The method uses a tapered glass tube, which narrows in its middle part to 2/3 of the diameter of the nucleus. The isolated nucleus is sucked into the narrow part of the capillary by gentle fluid movement, while the resulting change in electrical resistance is monitored. NE electrical conductance was unexpectedly large (7.9 +/- 0.34 S/cm(2)). Evaluation of NPC density by atomic force microscopy showed that this conductance corresponded to 3.7 x 10(6) NPCs. In contrast to earlier conclusions drawn from nuclear patch clamp experiments, NPCs were in an electrically "open" state with a mean single NPC electrical conductance of 1.7 +/- 0.07 nS. Enabling or blocking of active NPC transport (accomplished by the addition of cytosolic extracts or gp62-directed antibodies) revealed this large NPC conductance to be independent of the activation state of the transport machinery located in the center of NPCs. We conclude that peripheral channels, which are presumed to reside in the NPC subunits, establish a high ionic permeability that is virtually independent of the active protein transport mechanism.
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