ArticleThe EMBO journal2012
Sumoylation regulates Kap114-mediated nuclear transport.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Bound for the nucleus: defining the molecular principles of cargo selection by importin 9.bioRxiv : the preprint server for biology · 2026Article
- Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein.Nature communications · 2023Article
- Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Karyopherin-mediated nucleocytoplasmic transport.Nature reviews. Molecular cell biology · 2022Review
- Nuclear dynamics: Formation of bodies and trafficking in plant nuclei.Frontiers in plant science · 2022Review
- Light and shadow on the mechanisms of integration site selection in yeast Ty retrotransposon families.Current genetics · 2021Review
- Protein Sumoylation Is Crucial for Phagocytosis inInternational journal of molecular sciences · 2021Article
- Karyopherin Kap114p-mediated trans-repression controls ribosomal gene expression under saline stress.EMBO reports · 2020Article
- Acetylation modulates thyroid hormone receptor intracellular localization and intranuclear mobility.Molecular and cellular endocrinology · 2019Article
- SUMOylation of the nuclear pore complex basket is involved in sensing cellular stresses.Journal of cell science · 2019Article
- Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2.Nature communications · 2018Article
- A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits.Nature communications · 2018Article
- Interplay between Top1 and Mms21/Nse2 mediated sumoylation in stable maintenance of long chromosomes.Current genetics · 2017Article
- A high throughput mutagenic analysis of yeast sumo structure and function.PLoS genetics · 2017Article
- Article
- Sumoylation of the GTPase Ran by the RanBP2 SUMO E3 Ligase Complex.The Journal of biological chemistry · 2015Article
- Article
- A RanGTP-independent mechanism allows ribosomal protein nuclear import for ribosome assembly.eLife · 2014Article
- The SUMO proteases SENP1 and SENP2 play a critical role in nucleoporin homeostasis and nuclear pore complex function.Molecular biology of the cell · 2014Article
- SUMO unloads the Kap114 cab.The EMBO journal · 2012Article
Corrections and comments
- Commented on by
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear import receptor Kap114 carries transcription factors and other cargos across nuclear pores into the nucleus. Here we show that yeast Kap114 is modified by SUMO (small ubiquitin-related modifier) and that sumoylation is required for Kap114-mediated nuclear import. Among the four known SUMO-specific E3 ligases in yeast, Mms21 is the preferred E3 enzyme responsible for the covalent attachment of SUMO to the Kap114 protein. Kap114 is sumoylated on lysine residue 909, which is part of a ΨKxD/E sumoylation consensus motif. Kap114 containing a lysine-to-arginine point mutation at position 909 mislocalizes to the nucleus and is defective in promoting nuclear import. Similarly, mutants defective in sumoylation or desumoylation specifically accumulate Kap114 in the nucleus and are blocked in import of Kap114 cargos. Ran-GTP is not sufficient to disassemble Kap114/cargo complexes, which necessitates additional cargo release mechanisms in the nucleus. Remarkably, sumoylation of Kap114 greatly stimulates cargo dissociation in vitro. We propose that sumoylation occurs at the site of Kap114 cargo function and that SUMO is a cargo release factor involved in intranuclear targeting.
Indexed as
Identifiers
What OpenQuestion holds
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.