ArticleMolecular and cellular biology2002
Activation of the Bur1-Bur2 cyclin-dependent kinase complex by Cak1.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 51 citations in OpenAlex.
- Article
- Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023Review
- Acute stress drives global repression through two independent RNA polymerase II stalling events in Saccharomyces.Cell reports · 2021Article
- A SUMO-dependent pathway controls elongating RNA Polymerase II upon UV-induced damage.Scientific reports · 2019Article
- Gene modification by fast-track recombineering for cellular localization and isolation of components of plant protein complexes.The Plant journal : for cell and molecular biology · 2019Article
- The telomeric Cdc13-Stn1-Ten1 complex regulates RNA polymerase II transcription.Nucleic acids research · 2019Article
- Cdk7: a kinase at the core of transcription and in the crosshairs of cancer drug discovery.Transcription · 2019Review
- Functional interaction of Rpb1 and Spt5 C-terminal domains in co-transcriptional histone modification.Nucleic acids research · 2015Article
- The many roles of the conserved eukaryotic Paf1 complex in regulating transcription, histone modifications, and disease states.Biochimica et biophysica acta · 2013Article
- The CDK Network: Linking Cycles of Cell Division and Gene Expression.Genes & cancer · 2012Article
- Cyclin-dependent kinase control of the initiation-to-elongation switch of RNA polymerase II.Nature structural & molecular biology · 2012Article
- Cdk9 T-loop phosphorylation is regulated by the calcium signaling pathway.Journal of cellular physiology · 2012Article
- Dissecting phosphorylation networks: lessons learned from yeast.Expert review of proteomics · 2011Review
- Sporulation in the budding yeast Saccharomyces cerevisiae.Genetics · 2011Review
- An investigation of a role for U2 snRNP spliceosomal components in regulating transcription.PloS one · 2011Article
- Bringing order to protein disorder through comparative genomics and genetic interactions.Genome biology · 2011Article
- Identifying human kinase-specific protein phosphorylation sites by integrating heterogeneous information from various sources.PloS one · 2010Article
- Sub1 globally regulates RNA polymerase II C-terminal domain phosphorylation.Molecular and cellular biology · 2010Article
- A Plasmodium falciparum transcriptional cyclin-dependent kinase-related kinase with a crucial role in parasite proliferation associates with histone deacetylase activity.Eukaryotic cell · 2010Article
- A phosphorylation-independent role for the yeast cyclin-dependent kinase activating kinase Cak1.Gene · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cyclin-dependent kinases (Cdks) were originally identified as regulators of eukaryotic cell cycle progression, but several Cdks were subsequently shown to perform important roles as transcriptional regulators. While the mechanisms regulating the Cdks involved in cell cycle progression are well documented, much less is known regarding how the Cdks that are involved in transcription are regulated. In Saccharomyces cerevisiae, Bur1 and Bur2 comprise a Cdk complex that is involved in transcriptional regulation, presumably mediated by its phosphorylation of the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II. To investigate the regulation of Bur1 in vivo, we searched for high-copy-number suppressors of a bur1 temperature-sensitive mutation, identifying a single gene, CAK1. Cak1 is known to activate two other Cdks in yeast by phosphorylating a threonine within their conserved T-loop domains. Bur1 also has the conserved threonine within its T loop and is therefore a potential direct target of Cak1. Additional tests establish a direct functional interaction between Cak1 and the Bur1-Bur2 Cdk complex: Bur1 is phosphorylated in vivo, both the conserved Bur1 T-loop threonine and Cak1 are required for phosphorylation and Bur1 function in vivo, and recombinant Cak1 stimulates CTD kinase activity of the purified Bur1-Bur2 complex in vitro. Thus, both genetic and biochemical evidence demonstrate that Cak1 is a physiological regulator of the Bur1 kinase.
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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.