ArticleEMBO reports2006
Nuclear export modulates the cytoplasmic Sir2 homologue Hst2.
Article in EMBO reports, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed, 53 citations in OpenAlex.
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- Microtubule acetylation dyshomeostasis in Parkinson's disease.Translational neurodegeneration · 2023Review
- Systematic characterization ofFrontiers in microbiology · 2023Article
- SIRT2 promotes the viability, invasion and metastasis of osteosarcoma cells by inhibiting the degradation of Snail.Cell death & disease · 2022Article
- Contributions of a Histone Deacetylase (SirT2/Hst2) toJournal of fungi (Basel, Switzerland) · 2022Article
- The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy.Frontiers in cell and developmental biology · 2020Review
- A synthetic non-histone substrate to study substrate targeting by the Gcn5 HAT and sirtuin HDACs.The Journal of biological chemistry · 2019Article
- Article
- Reduced expression of SIRT2 in serous ovarian carcinoma promotes cell proliferation through disinhibition of CDK4 expression.Molecular medicine reports · 2017Article
- HST1 increases replicative lifespan of a sir2Δ mutant in the absence of PDE2 in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2017Article
- Nicotinamide Suppresses the DNA Damage Sensitivity of Saccharomyces cerevisiae Independently of Sirtuin Deacetylases.Genetics · 2016Article
- Chromosome-wide histone deacetylation by sirtuins prevents hyperactivation of DNA damage-induced signaling upon replicative stress.Nucleic acids research · 2016Article
- Less is more: Nutrient limitation induces cross-talk of nutrient sensing pathways with NADFrontiers in biology · 2015Article
- Sirtuins in epigenetic regulation.Chemical reviews · 2015Review
- Acetylome profiling reveals overlap in the regulation of diverse processes by sirtuins, gcn5, and esa1.Molecular & cellular proteomics : MCP · 2015Article
- Regulation of NAD+ metabolism, signaling and compartmentalization in the yeast Saccharomyces cerevisiae.DNA repair · 2014Review
- Sirtuins in stress response: guardians of the genome.Oncogene · 2014Review
- Yeast sirtuins and the regulation of aging.FEMS yeast research · 2014Review
- Gcn5 and sirtuins regulate acetylation of the ribosomal protein transcription factor Ifh1.Current biology : CB · 2013Article
- Emerging role of sirtuins on tumorigenesis: possible link between aging and cancer.BMB reports · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modulating transcription factors is crucial to executing sophisticated gene expression programs. The silent information regulator 2 (Sir2) family of NAD-dependent protein deacetylases influences transcription by targeting proteins such as histones, p53 and forkhead-box family transcription factors. Although apparently cytoplasmic, both mammalian SIRT2 and its yeast orthologue Hst2 have been implicated in transcriptional regulation. Here, we show that Hst2 moves between the nucleus and cytoplasm, but is largely cytoplasmic owing to efficient nuclear export. This nuclear exclusion is mediated by the exportin chromosomal region maintenance 1 (Crm1) and a putative leucine-rich nuclear export sequence in Hst2, which overlaps a unique autoregulatory helix. Disruption of Hst2 export shows that nuclear exclusion inhibits the activity of Hst2 as a transcriptional repressor. Our identification of putative nuclear export sequences in numerous vertebrate SIRT2 proteins shows that active nuclear export can be a conserved mechanism for regulating Sir2 homologues.
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Registered trials
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.