ArticleBiochemical and biophysical research communications2007
The Dcr2p phosphatase destabilizes Sic1p in Saccharomyces cerevisiae.
Article in Biochemical and biophysical research communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- A novel mechanism for the retention of Golgi membrane proteins mediated by the Bre5p/Ubp3p deubiquitinase complex.Molecular biology of the cell · 2020Article
- The effective application of a discrete transition model to explore cell-cycle regulation in yeast.BMC research notes · 2013Article
- Distinct interactions select and maintain a specific cell fate.Molecular cell · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Initiation of cell division is controlled by an irreversible switch. In Saccharomyces cerevisiae degradation of the Sic1p protein, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, takes place before initiation of DNA replication, at a point called START. Sic1p is phosphorylated by multiple kinases, which can differentially affect the stability of Sic1p. How phosphorylations that stabilize Sic1p are reversed is unknown. Here we show that the Dcr2p phosphatase functionally and physically interacts with Sic1p. Over-expression of Dcr2p destabilizes Sic1p and leads to phenotypes associated with destabilized Sic1p, such as genome instability. Our results identify a novel factor that affects the stability of Sic1p, possibly contributing to mechanisms that trigger initiation of cell division.
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