ArticleThe Journal of membrane biology1995
Patch clamp detection of transcription factor translocation along the nuclear pore complex channel.
Article in The Journal of membrane biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 30 citations in OpenAlex.
- Activation of intracellular calcium by multiple Wnt ligands and translocation of β-catenin into the nucleus: a convergent model of Wnt/Ca2+ and Wnt/β-catenin pathways.The Journal of biological chemistry · 2013Article
- Passive transport of macromolecules through Xenopus laevis nuclear envelope.The Journal of membrane biology · 2003Article
- Dendrimer-assisted patch-clamp sizing of nuclear pores.Pflugers Archiv : European journal of physiology · 2000Article
- Calcium, ATP and nuclear pore channel gating.Pflugers Archiv : European journal of physiology · 2000Article
- Microsecond time-scale discrimination among polycytidylic acid, polyadenylic acid, and polyuridylic acid as homopolymers or as segments within single RNA molecules.Biophysical journal · 1999Article
- ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis.Biophysical journal · 1998Article
- Identification and characterization of a cell membrane nucleic acid channel.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Characterization of individual polynucleotide molecules using a membrane channel.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- The ion channel behavior of the nuclear pore complex.The Journal of membrane biology · 1995Article
- Patch clamp and atomic force microscopy demonstrate TATA-binding protein (TBP) interactions with the nuclear pore complex.The Journal of membrane biology · 1995Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription factors (TFs) are cytoplasmic proteins that play an essential role in gene expression. These proteins form multimers and this phenomenon is thought to be one of the mechanisms that regulate transcription. TF molecules reach their DNA binding sites through the large central channel of the nuclear pore complex (NPC). However, the NPC channel is known to restrict the translocation of molecules > or = 20-70 kD. Therefore, during their translocation, TF molecules and/or their multimers may plug the NPC channel and thus, interrupt ion flow through the channel, with a concomitant reduction in the ion conductance of the channel (gamma). Here we show with patch clamp that gamma is reduced during translocation of three major TFs: c-Jun (40 kD), NF-kappa B (approximately equal to 50 kD), and SP1 (approximately equal to 100 kD). Within a minute, femtomolar concentrations of these proteins reduced gamma suggesting a purely mechanical interaction between single TF molecules and the inner wall of the NPC channel. NPCs remained plugged for 0.5-3 hr in the absence of ATP but when ATP was added, channel plugging was shortened to < 5 min. After unplugging, channel closures were rarely observed and the number of functional channels increased. The transcription factors also stabilized the NPCs as shown by the extended duration of the preparations which allowed recordings for up to 72 hr. These observations are the first direct demonstration of the important role of NPCs in mediating nuclear translocation of TFs and, therefore, in forming part of the mechanisms regulating gene expression.(ABSTRACT TRUNCATED AT 250 WORDS)
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