ArticleGenes & development2009
The SESA network links duplication of the yeast centrosome with the protein translation machinery.
Article in Genes & development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed, 79 citations in OpenAlex.
- Med9 Is a Novel eIF4E-Interacting Protein inInternational journal of molecular sciences · 2026Article
- Identification of RNA-Binding Protein Targets with HyperTRIBE inInternational journal of molecular sciences · 2023Article
- Yeast Smy2 and its human homologs GIGYF1 and -2 regulate Cdc48/VCP function during transcription stress.Cell reports · 2022Article
- Distinct elongation stalls during translation are linked with distinct pathways for mRNA degradation.eLife · 2022Article
- HDLBP binds ER-targeted mRNAs by multivalent interactions to promote protein synthesis of transmembrane and secreted proteins.Nature communications · 2022Article
- A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit.International journal of molecular sciences · 2021Article
- Article
- eIF4E and Interactors from Unicellular Eukaryotes.International journal of molecular sciences · 2020Review
- Local translation of yeastRNA (New York, N.Y.) · 2019Article
- Asymmetric distribution of glucose transporter mRNA provides a growth advantage in yeast.The EMBO journal · 2019Article
- Yeast centrosome components form a noncanonical LINC complex at the nuclear envelope insertion site.The Journal of cell biology · 2019Article
- Expression of TorsinA in a heterologous yeast system reveals interactions with lumenal domains of LINC and nuclear pore complex components.Molecular biology of the cell · 2019Article
- Translational regulation in response to stress in Saccharomyces cerevisiae.Yeast (Chichester, England) · 2019Review
- Review
- N-terminal Acetylation Levels Are Maintained During Acetyl-CoA Deficiency inMolecular & cellular proteomics : MCP · 2018Article
- The budding yeast RSC complex maintains ploidy by promoting spindle pole body insertion.The Journal of cell biology · 2018Article
- Review
- Capturing the Asc1p/Molecular & cellular proteomics : MCP · 2017Article
- Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.The Journal of cell biology · 2017Article
- ATX-2, the C. elegans Ortholog of Human Ataxin-2, Regulates Centrosome Size and Microtubule Dynamics.PLoS genetics · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast spindle pole body (SPB), the functional equivalent of mammalian centrosome, duplicates in G1/S phase of the cell cycle and then becomes inserted into the nuclear envelope. Here we describe a link between SPB duplication and targeted translation control. When insertion of the newly formed SPB into the nuclear envelope fails, the SESA network comprising the GYF domain protein Smy2, the translation inhibitor Eap1, the mRNA-binding protein Scp160 and the Asc1 protein, specifically inhibits initiation of translation of POM34 mRNA that encodes an integral membrane protein of the nuclear pore complex, while having no impact on other mRNAs. In response to SESA, POM34 mRNA accumulates in the cytoplasm and is not targeted to the ER for cotranslational translocation of the protein. Reduced level of Pom34 is sufficient to restore viability of mutants with defects in SPB duplication. We suggest that the SESA network provides a mechanism by which cells can regulate the translation of specific mRNAs. This regulation is used to coordinate competing events in the nuclear envelope.
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.