ArticleMolecular biology of the cell1998
Phosphorylation of sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk including Pho85 kinase is required for its prompt degradation.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 105 citations in OpenAlex.
- The CDK Pho85 inhibits Whi7 Start repressor to promote cell cycle entry in budding yeast.EMBO reports · 2024Article
- Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023Review
- Analog-sensitive Cdk1 as a tool to study mitotic exit: protein phosphatase 1 is required downstream from Cdk1 inactivation in budding yeast.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023Article
- Exit from Mitosis in Budding Yeast: Protein Phosphatase 1 is Required Downstream from Cdk1 Inactivation.Research square · 2023Article
- Redundant targeting of Isr1 by two CDKs in mitotic cells.Current genetics · 2021Review
- Review
- Protein Phosphatases in G1 Regulation.International journal of molecular sciences · 2020Review
- A comprehensive, mechanistically detailed, and executable model of the cell division cycle in Saccharomyces cerevisiae.Nature communications · 2019Article
- An Antimicrobial Peptide InducesFrontiers in microbiology · 2018Article
- Two maize Kip-related proteins differentially interact with, inhibit and are phosphorylated by cyclin D-cyclin-dependent kinase complexes.Journal of experimental botany · 2017Article
- New structural insights into phosphorylation-free mechanism for full cyclin-dependent kinase (CDK)-cyclin activity and substrate recognition.The Journal of biological chemistry · 2013Article
- Redundancy or specificity? The role of the CDK Pho85 in cell cycle control.International journal of biochemistry and molecular biology · 2013Review
- The effective application of a discrete transition model to explore cell-cycle regulation in yeast.BMC research notes · 2013Article
- CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression.Cell · 2012Article
- The importance of conserved features of yeast actin-binding protein 1 (Abp1p): the conditional nature of essentiality.Genetics · 2012Article
- Evolution of networks and sequences in eukaryotic cell cycle control.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011Review
- Dynamics of Cdk1 substrate specificity during the cell cycle.Molecular cell · 2011Article
- SCFCdc4 enables mating type switching in yeast by cyclin-dependent kinase-mediated elimination of the Ash1 transcriptional repressor.Molecular and cellular biology · 2011Article
- Multisite phosphorylation provides an effective and flexible mechanism for switch-like protein degradation.PloS one · 2010Article
- Positive or negative roles of different cyclin-dependent kinase Pho85-cyclin complexes orchestrate induction of autophagy in Saccharomyces cerevisiae.Molecular cell · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the yeast Saccharomyces cerevisiae, Sic1, an inhibitor of Clb-Cdc28 kinases, must be phosphorylated and degraded in G1 for cells to initiate DNA replication, and Cln-Cdc28 kinase appears to be primarily responsible for phosphorylation of Sic1. The Pho85 kinase is a yeast cyclin-dependent kinase (Cdk), which is not essential for cell growth unless both CLN1 and CLN2 are absent. We demonstrate that Pho85, when complexed with Pcl1, a G1 cyclin homologue, can phosphorylate Sic1 in vitro, and that Sic1 appears to be more stable in pho85Delta cells. Three consensus Cdk phosphorylation sites present in Sic1 are phosphorylated in vivo, and two of them are required for prompt degradation of the inhibitor. Pho85 and other G1 Cdks appear to phosphorylate Sic1 at different sites in vivo. Thus at least two distinct Cdks can participate in phosphorylation of Sic1 and may therefore regulate progression through G1.
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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.