ArticleThe Journal of cell biology2017
Yeast silencing factor Sir4 and a subset of nucleoporins form a complex distinct from nuclear pore complexes.
Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Ctf18-dependent localization of interstitial telomeric sequence to nuclear pore complexes prevents chromosome fragility.Nucleic acids research · 2026Article
- The ubiquitin protease Ubp10 suppresses the formation of translocations at interstitial telomere-like sites.Nucleic acids research · 2025Article
- Transcriptional condensates and the nuclear pore complex regulate gene expression and 3D genome architecture in response to stress.Biochemical Society transactions · 2025Review
- Ulp1 association with nuclear pore complexes is required for the maintenance of global SUMOylation.Molecular biology of the cell · 2025Article
- Review
- Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- You are who your friends are-nuclear pore proteins as components of chromatin-binding complexes.FEBS letters · 2023Review
- Nuclear pore complexes mediate subtelomeric gene silencing by regulating PCNA levels on chromatin.The Journal of cell biology · 2023Article
- SUMOylation at the inner nuclear membrane facilitates nuclear envelope biogenesis during mitosis.The Journal of cell biology · 2023Article
- Review
- The regional sequestration of heterochromatin structural proteins is critical to form and maintain silent chromatin.Epigenetics & chromatin · 2022Review
- The Nuclear Pore Complex as a Transcription Regulator.Cold Spring Harbor perspectives in biology · 2022Review
- Phosphorylation-dependent mitotic SUMOylation drives nuclear envelope-chromatin interactions.The Journal of cell biology · 2021Article
- A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription.PLoS genetics · 2021Article
- The challenge of staying in shape: nuclear size matters.Current genetics · 2021Review
- One Ring to Rule them All? Structural and Functional Diversity in the Nuclear Pore Complex.Trends in biochemical sciences · 2021Review
- Article
- The nuclear pore complex and the genome: organizing and regulatory principles.Current opinion in genetics & development · 2021Review
- Native Chromatin Proteomics Reveals a Role for Specific Nucleoporins in Heterochromatin Organization and Maintenance.Molecular cell · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Interactions occurring at the nuclear envelope (NE)-chromatin interface influence both NE structure and chromatin organization. Insights into the functions of NE-chromatin interactions have come from the study of yeast subtelomeric chromatin and its association with the NE, including the identification of various proteins necessary for tethering subtelomeric chromatin to the NE and the silencing of resident genes. Here we show that four of these proteins-the silencing factor Sir4, NE-associated Esc1, the SUMO E3 ligase Siz2, and the nuclear pore complex (NPC) protein Nup170-physically and functionally interact with one another and a subset of NPC components (nucleoporins or Nups). Importantly, this group of Nups is largely restricted to members of the inner and outer NPC rings, but it lacks numerous others including cytoplasmically and nucleoplasmically positioned Nups. We propose that this Sir4-associated Nup complex is distinct from holo-NPCs and that it plays a role in subtelomeric chromatin organization and NE tethering.
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Registered trials
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