ArticleMolecular and cellular biology1999
Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the cyclin Pcl10p.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 57 citations in OpenAlex.
- The nutrient-responsive CDK Pho85 primes the Sch9 kinase for its activation by TORC1.PLoS genetics · 2023Article
- TheFrontiers in microbiology · 2022Article
- Article
- Functional Analysis of Kinases and Transcription Factors inG3 (Bethesda, Md.) · 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
- Acid phosphatases of budding yeast as a model of choice for transcription regulation research.Enzyme research · 2011Article
- Regulation of glycogen metabolism in yeast and bacteria.FEMS microbiology reviews · 2010Review
- The subcellular localization of yeast glycogen synthase is dependent upon glycogen content.Canadian journal of microbiology · 2010Article
- Identity of the growth-limiting nutrient strongly affects storage carbohydrate accumulation in anaerobic chemostat cultures of Saccharomyces cerevisiae.Applied and environmental microbiology · 2009Article
- Dual regulation by pairs of cyclin-dependent protein kinases and histone deacetylases controls G1 transcription in budding yeast.PLoS biology · 2009Article
- Degradation of Saccharomyces cerevisiae transcription factor Gcn4 requires a C-terminal nuclear localization signal in the cyclin Pcl5.Eukaryotic cell · 2009Article
- Nutrient-regulated antisense and intragenic RNAs modulate a signal transduction pathway in yeast.PLoS biology · 2008Article
- Autophosphorylation-induced degradation of the Pho85 cyclin Pcl5 is essential for response to amino acid limitation.Molecular and cellular biology · 2008Article
- Yeast Gcn4p stabilization is initiated by the dissociation of the nuclear Pho85p/Pcl5p complex.Molecular biology of the cell · 2006Article
- Control of mammalian glycogen synthase by PAS kinase.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The minimum domain of Pho81 is not sufficient to control the Pho85-Rim15 effector branch involved in phosphate starvation-induced stress responses.Current genetics · 2005Article
- Coevolution of cyclin Pcl5 and its substrate Gcn4.Eukaryotic cell · 2005Article
- Combinatorial control by the protein kinases PKA, PHO85 and SNF1 of transcriptional induction of the Saccharomyces cerevisiae GSY2 gene at the diauxic shift.Molecular genetics and genomics : MGG · 2004Article
- Article
- CTD kinase I is involved in RNA polymerase I transcription.Nucleic acids research · 2004Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
In Saccharomyces cerevisiae, PHO85 encodes a cyclin-dependent protein kinase (Cdk) catalytic subunit with multiple regulatory roles thought to be specified by association with different cyclin partners (Pcls). Pcl10p is one of four Pcls with little sequence similarity to cyclins involved in cell cycle control. It has been implicated in specifying the phosphorylation of glycogen synthase (Gsy2p). We report that recombinant Pho85p and Pcl10p produced in Escherichia coli reconstitute an active Gsy2p kinase in vitro. Gsy2p phosphorylation required Pcl10p, occurred at physiologically relevant sites, and resulted in inactivation of Gsy2p. The activity of the reconstituted enzyme was even greater than Pho85p-Pcl10p isolated from yeast, and we conclude that, unlike many Cdks, Pho85p does not require phosphorylation for activity. Pcl10p formed complexes with Gsy2p, as judged by (i) gel filtration of recombinant Pcl10p and Gsy2p, (ii) coimmunoprecipitation from yeast cell lysates, and (iii) enzyme kinetic behavior consistent with Pcl10p binding the substrate. Synthetic peptides modeled on the sequences of known Pho85p sites were poor substrates with high K(m) values, and we propose that Pcl10p-Gsy2p interaction is important for substrate selection. Gel filtration of yeast cell lysates demonstrated that most Pho85p was present as a monomer, although a portion coeluted in high-molecular-weight fractions with Pcl10p and Gsy2p. Overexpression of Pcl10p sequestered most of the Pho85p into association with Pcl10p. We suggest a model for Pho85p function in the cell whereby cyclins like Pcl10p recruit Pho85p from a pool of monomers, both activating the kinase and targeting it to substrate.
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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.