ArticleMolecular and cellular biology2010
Activation of the S-phase checkpoint inhibits degradation of the F-box protein Dia2.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- SKP1-CUL1-F-box: Key molecular targets affecting disease progression.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Review
- The Effect of Dia2 Protein Deficiency on the Cell Cycle, Cell Size, and Recruitment of Ctf4 Protein inMolecules (Basel, Switzerland) · 2021Article
- Interaction between Brassica yellows virus silencing suppressor P0 and plant SKP1 facilitates stability of P0 in vivo against degradation by proteasome and autophagy pathways.The New phytologist · 2019Article
- Degradation of Mrc1 promotes recombination-mediated restart of stalled replication forks.Nucleic acids research · 2017Article
- Proteasome-dependent degradation of replisome components regulates faithful DNA replication.Cell cycle (Georgetown, Tex.) · 2013Review
- The Saccharomyces cerevisiae F-box protein Dia2 is a mediator of S-phase checkpoint recovery from DNA damage.Genetics · 2013Article
- Hect E3 ubiquitin ligase Tom1 controls Dia2 degradation during the cell cycle.Molecular biology of the cell · 2012Article
- The ubiquitin-proteasome system of Saccharomyces cerevisiae.Genetics · 2012Review
- WNP: a novel algorithm for gene products annotation from weighted functional networks.PloS one · 2012Article
- Article
- Hsk1- and SCF(Pof3)-dependent proteolysis of S. pombe Ams2 ensures histone homeostasis and centromere function.Developmental cell · 2010Article
- The replication stress response and the ubiquitin system: a new link in maintaining genomic integrity.Cell division · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A stable genome is critical to cell viability and proliferation. During DNA replication, the S-phase checkpoint pathway responds to replication stress. In budding yeast, the chromatin-bound F-box protein Dia2 is required to maintain genomic stability and may help replication complexes overcome sites of damaged DNA and natural fragile regions. SCF (Skp1/Cul1/F-box protein) complexes are modular ubiquitin ligases. We show here that Dia2 is itself targeted for ubiquitin-mediated proteolysis and that activation of the S-phase checkpoint pathway inhibits Dia2 protein degradation. S-phase checkpoint mutants fail to stabilize Dia2 in response to replication stress. Deletion of DIA2 from these checkpoint mutants exacerbates their sensitivity to hydroxyurea, suggesting that stabilization of Dia2 contributes to the replication stress response. Unlike the case for other F-box proteins, deletion of the F-box domain in Dia2 does not stabilize the protein. Rather, an N-terminal domain that is also required for nuclear localization is necessary for degradation. When a strong nuclear localization signal (NLS) is added to dia2 mutants lacking this domain, the Dia2 protein is both stable and nuclear. Together, our results suggest that Dia2 protein turnover does not involve an autocatalytic mechanism and that Dia2 proteolysis is inhibited by activation of the replication stress response.
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