ArticleMolecular biology of the cell1997
Ran1 functions to control the Cdc10/Sct1 complex through Puc1.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Lessons on fruiting body morphogenesis from genomes and transcriptomes ofStudies in mycology · 2023Article
- DSC1-MCB regulation of meiotic transcription in Schizosaccharomyces pombe.Molecular genetics and genomics : MGG · 2004Article
- Gene expression profile of HIV-1 Tat expressing cells: a close interplay between proliferative and differentiation signals.BMC biochemistry · 2002Article
- Cell cycle-regulated transcription in fission yeast: Cdc10-Res protein interactions during the cell cycle and domains required for regulated transcription.Molecular biology of the cell · 1999Article
- Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 1998Review
- The fission yeast protein p73res2 is an essential component of the mitotic MBF complex and a master regulator of meiosis.Molecular and cellular biology · 1997Article
- The Cdc2 protein kinase controls Cdc10/Sct1 complex formation.Molecular biology of the cell · 1997Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have undertaken a biochemical analysis of the regulation of the G1/S-phase transition and commitment to the cell cycle in the fission yeast Schizosaccharomyces pombe. The execution of Start requires the activity of the Cdc2 protein kinase and the Sct1/Cdc10 transcription complex. Progression through G1 also requires the Ran1 protein kinase whose inactivation leads to activation of the meiotic pathway under conditions normally inhibitory to this process. We have found that in addition to Cdc2, Sct1/Cdc10 complex formation requires Ran1. We demonstrate that the Puc1 cyclin associates with Ran1 and Cdc10 in vivo and that the Ran1 protein kinase functions to control the association between Puc1 and Cdc10. In addition, we present evidence that the phosphorylation state of Cdc10 is altered upon inactivation of Ran1. These results provide biochemical evidence that demonstrate one mechanism by which the Ran1 protein kinase serves to control cell fate through Cdc10 and Puc1.
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