ArticlePloS one2011
The nuclear pore complex mediates binding of the Mig1 repressor to target promoters.
Article in PloS one, 2011. 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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Who cites it
10 citing papers in PubMed, 40 citations in OpenAlex.
- The polyHIS Tract of Yeast AMPK Coordinates Carbon Metabolism with Iron Availability.International journal of molecular sciences · 2023Article
- A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription.PLoS genetics · 2021Article
- Genetic interaction network has a very limited impact on the evolutionary trajectories in continuous culture-grown populations of yeast.BMC ecology and evolution · 2021Article
- HOXA repression is mediated by nucleoporin Nup93 assisted by its interactors Nup188 and Nup205.Epigenetics & chromatin · 2016Article
- Sumoylation and transcription regulation at nuclear pores.Chromosoma · 2015Review
- Nuclear pore proteins and the control of genome functions.Genes & development · 2015Review
- Nuclear routing networks span between nuclear pore complexes and genomic DNA to guide nucleoplasmic trafficking of biomolecules.Journal of fertilization in vitro · 2012Article
- Routing of Biomolecules and Transgenes' Vectors in Nuclei of Oocytes.Journal of fertilization in vitro · 2012Article
- A negative feedback loop at the nuclear periphery regulates GAL gene expression.Molecular biology of the cell · 2012Article
- The new nucleoporin: regulator of transcriptional repression and beyond.Nucleus (Austin, Tex.)Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
All eukaryotic cells alter their transcriptional program in response to the sugar glucose. In Saccharomyces cerevisiae, the best-studied downstream effector of this response is the glucose-regulated repressor Mig1. We show here that nuclear pore complexes also contribute to glucose-regulated gene expression. NPCs participate in glucose-responsive repression by physically interacting with Mig1 and mediating its function independently of nucleocytoplasmic transport. Surprisingly, despite its abundant presence in the nucleus of glucose-grown nup120Δ or nup133Δ cells, Mig1 has lost its ability to interact with target promoters. The glucose repression defect in the absence of these nuclear pore components therefore appears to result from the failure of Mig1 to access its consensus recognition sites in genomic DNA. We propose that the NPC contributes to both repression and activation at the level of transcription.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.