ArticleMolecular biology of the cell2012
Hect E3 ubiquitin ligase Tom1 controls Dia2 degradation during the cell cycle.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 19 citations in OpenAlex.
- Lysine deficiency within a conserved lysine desert is critical for EEL-1/HUWE1 to support ubiquitin proteasome system function.PLoS genetics · 2026Article
- Lysine deficiency within a conserved lysine desert is critical for EEL-1/HUWE1 to support ubiquitin proteasome system function.bioRxiv : the preprint server for biology · 2025Article
- Dot6/Tod6 degradation fine-tunes the repression of ribosome biogenesis under nutrient-limited conditions.iScience · 2022Article
- Up-regulation of ubiquitin-proteasome activity upon loss of NatA-dependent N-terminal acetylation.Life science alliance · 2022Article
- HJournal of fungi (Basel, Switzerland) · 2021Article
- The Sir4 H-BRCT domain interacts with phospho-proteins to sequester and repress yeast heterochromatin.The EMBO journal · 2019Article
- Article
- The ribosome-bound quality control complex remains associated to aberrant peptides during their proteasomal targeting and interacts with Tom1 to limit protein aggregation.Molecular biology of the cell · 2017Article
- A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins.eLife · 2016Article
- Skp1 Independent Function of Cdc53/Cul1 in F-box Protein Homeostasis.PLoS genetics · 2015Article
- The SMC Loader Scc2 Promotes ncRNA Biogenesis and Translational Fidelity.PLoS genetics · 2015Article
- Article
- The Hect domain E3 ligase Tom1 and the F-box protein Dia2 control Cdc6 degradation in G1 phase.The Journal of biological chemistry · 2012Article
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2 authors at 1 institution in 1 country.
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Abstract
The ubiquitin proteasome system plays a pivotal role in controlling the cell cycle. The budding yeast F-box protein Dia2 is required for genomic stability and is targeted for ubiquitin-dependent degradation in a cell cycle-dependent manner, but the identity of the ubiquitination pathway is unknown. We demonstrate that the Hect domain E3 ubiquitin ligase Tom1 is required for Dia2 protein degradation. Deletion of DIA2 partially suppresses the temperature-sensitive phenotype of tom1 mutants. Tom1 is required for Dia2 ubiquitination and degradation during G1 and G2/M phases of the cell cycle, whereas the Dia2 protein is stabilized during S phase. We find that Tom1 binding to Dia2 is enhanced in G1 and reduced in S phase, suggesting a mechanism for this proteolytic switch. Tom1 recognizes specific, positively charged residues in a Dia2 degradation/NLS domain. Loss of these residues blocks Tom1-mediated turnover of Dia2 and causes a delay in G1-to-S phase progression. Deletion of DIA2 rescues a delay in the G1-to-S phase transition in the tom1Δ mutant. Together our results suggest that Tom1 targets Dia2 for degradation during the cell cycle by recognizing positively charged residues in the Dia2 degradation/NLS domain and that Dia2 protein degradation contributes to G1-to-S phase progression.
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