ArticlePloS one2011
Nutrient sensing kinases PKA and Sch9 phosphorylate the catalytic domain of the ubiquitin-conjugating enzyme Cdc34.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.
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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
10 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.
- The emerging roles of Jab1/CSN5 in cancer.Medical oncology (Northwood, London, England) · 2016Pooled it
- The Yeast Protein Kinase Sch9 Functions as a Central Nutrient-Responsive Hub That Calibrates Metabolic and Stress-Related Responses.Journal of fungi (Basel, Switzerland) · 2023Review
- Using the AKAR3-EV biosensor to assess Sch9p- and PKA-signalling in budding yeast.FEMS yeast research · 2023Article
- Activating the Anaphase Promoting Complex to Enhance Genomic Stability and Prolong Lifespan.International journal of molecular sciences · 2018Review
- Enzyme-substrate relationships in the ubiquitin system: approaches for identifying substrates of ubiquitin ligases.Cellular and molecular life sciences : CMLS · 2017Review
- The yeast protein kinase Sch9 adjusts V-ATPase assembly/disassembly to control pH homeostasis and longevity in response to glucose availability.PLoS genetics · 2017Article
- Control of APC/C-dependent ubiquitin chain elongation by reversible phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Sch9 regulates intracellular protein ubiquitination by controlling stress responses.Redox biology · 2015Article
- DNA replication stress-induced loss of reproductive capacity in S. cerevisiae and its inhibition by caloric restriction.Cell cycle (Georgetown, Tex.) · 2013Article
- Targeting Jab1/CSN5 in nasopharyngeal carcinoma.Cancer letters · 2012Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell division is controlled in part by the timely activation of the CDK, Cdc28, through its association with G1 and G2 cyclins. Cdc28 complexes are regulated in turn by the ubiquitin conjugating enzyme Cdc34 and SCF ubiquitin ligase complexes of the ubiquitin-proteasome system (UPS) to control the initiation of DNA replication. Here we demonstrate that the nutrient sensing kinases PKA and Sch9 phosphorylate S97 of Cdc34. S97 is conserved across species and restricted to the catalytic domain of Cdc34/Ubc7-like E2s. Cdc34-S97 phosphorylation is cell cycle regulated, elevated during active cell growth and division and decreased during cell cycle arrest. Cell growth and cell division are orchestrated to maintain cell size homeostasis over a wide range of nutrient conditions. Cells monitor changes in their environment through nutrient sensing protein kinases. Thus Cdc34 phosphorylation by PKA and Sch9 provides a direct tether between G1 cell division events and cell growth.
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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.