Phosphorylation by Cak1 Regulates the C-Terminal Domain Kinase Ctk1 in <i>Saccharomyces cerevisiae</i>

Ostapenko, Denis; Solomon, Mark J.

doi:10.1128/mcb.25.10.3906-3913.2005

Cited by 29 publications

(37 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…CDC28-dependent bypass of cak1 phenotypes but not ctf7 phenotypes: Cak1p phosphorylates many substrates including Kin28p, Bur1p, and Ctk1p, but the only essential role for Cak1p kinase is to activate Cdc28p (Espinoza et al 1996(Espinoza et al , 1998Cross and Levine 1998;Yao and Prelich 2002;Ostapenko and Solomon 2005;Ganem et al 2006). If the synthetic lethality that we observed between ctf7 and cak1 was in fact due to diminished CDK activation, we reasoned that Cak1p-bypass CDC28 alleles (Cross and Levine 1998) should rescue both cak1-277 temperature sensitivity and ctf7 cak1 synthetic lethality.…”

Section: Resultsmentioning

confidence: 99%

Sister Chromatid Cohesion Role for CDC28-CDK in Saccharomyces cerevisiae

Brands

Skibbens

2008

Genetics

View full text Add to dashboard Cite

High-fidelity chromosome segregation requires that the sister chromatids produced during S phase also become paired during S phase. Ctf7p (Eco1p) is required to establish sister chromatid pairing specifically during DNA replication. However, Ctf7p also becomes active during G 2 /M in response to DNA damage. Ctf7p is a phosphoprotein and an in vitro target of Cdc28p cyclin-dependent kinase (CDK), suggesting one possible mechanism for regulating the essential function of Ctf7p. Here, we report a novel synthetic lethal interaction between ctf7 and cdc28. However, neither elevated CDC28 levels nor CDC28 Cak1p-bypass alleles rescue ctf7 cell phenotypes. Moreover, cells expressing Ctf7p mutated at all full-and partial-consensus CDKphosphorylation sites exhibit robust cell growth. These and other results reveal that Ctf7p regulation is more complicated than previously envisioned and suggest that CDK acts in sister chromatid cohesion parallel to Ctf7p reactions.

show abstract

Section: Resultsmentioning

confidence: 99%

Sister Chromatid Cohesion Role for CDC28-CDK in Saccharomyces cerevisiae

Brands

Skibbens

2008

Genetics

View full text Add to dashboard Cite

show abstract

“…Hypomorphic mutations of the essential CAK1 or MPS1 genes produce spore wall defects similar to those seen in smk1 mutants, although unlike Smk1p, both of these kinases have distinct functions earlier in sporulation (19,148,150,161,177). In vegetative cells, CAK1 is required for phosphorylation of Cdc28p and other cyclin-dependent kinases on a threonine in an analogous position to the activating phosphorylation sites in Smk1p (37,69,117,184). Smk1p is not phosphorylated in a cak1 hypomorphic mutant (148).…”

Section: Vol 69 2005 Ascospore Formation In Saccharomyces Cerevisiamentioning

confidence: 99%

Ascospore Formation in the YeastSaccharomyces cerevisiae

Neiman

2005

Microbiol Mol Biol Rev

220

237

View full text Add to dashboard Cite

SUMMARY Sporulation of the baker's yeast Saccharomyces cerevisiae is a response to nutrient depletion that allows a single diploid cell to give rise to four stress-resistant haploid spores. The formation of these spores requires a coordinated reorganization of cellular architecture. The construction of the spores can be broadly divided into two phases. The first is the generation of new membrane compartments within the cell cytoplasm that ultimately give rise to the spore plasma membranes. Proper assembly and growth of these membranes require modification of aspects of the constitutive secretory pathway and cytoskeleton by sporulation-specific functions. In the second phase, each immature spore becomes surrounded by a multilaminar spore wall that provides resistance to environmental stresses. This review focuses on our current understanding of the cellular rearrangements and the genes required in each of these phases to give rise to a wild-type spore.

show abstract

“…Thus, previous studies demonstrated that Cak1 phosphorylates Kin28, Bur1, and Ctk1 within their T loops and stimulates their activities (22,36,52,72). Therefore, we tested whether Cak1 levels were altered in the absence of SUB1.…”

Section: (D)mentioning

confidence: 99%

Sub1 Globally Regulates RNA Polymerase II C-Terminal Domain Phosphorylation

García

Rosonina

Manley

et al. 2010

Molecular and Cellular Biology

View full text Add to dashboard Cite

The transcriptional coactivator Sub1 has been implicated in several aspects of mRNA metabolism in yeast, such as activation of transcription, termination, and 3-end formation. Here, we present evidence that Sub1 plays a significant role in controlling phosphorylation of the RNA polymerase II large subunit C-terminal domain (CTD). We show that SUB1 genetically interacts with the genes encoding all four known CTD kinases, SRB10, KIN28, BUR1, and CTK1, suggesting that Sub1 acts to influence CTD phosphorylation at more than one step of the transcription cycle. To address this directly, we first used in vitro kinase assays, and we show that, on the one hand, SUB1 deletion increased CTD phosphorylation by Kin28, Bur1, and Ctk1 but, on the other, it decreased CTD phosphorylation by Srb10. Second, chromatin immunoprecipitation assays revealed that SUB1 deletion decreased Srb10 chromatin association on the inducible GAL1 gene but increased Kin28 and Ctk1 chromatin association on actively transcribed genes. Taken together, our data point to multiple roles for Sub1 in the regulation of CTD phosphorylation throughout the transcription cycle.A prominent feature of the largest subunit of RNA polymerase II (RNAP II), Rpb1, is the presence of a highly conserved carboxy-terminal domain (CTD) that has an essential role in transcription regulation in vivo (12,17,54). Although the RNAP II CTD is not required for transcription in promoterindependent assays in vitro, it is essential in vivo (50), and it is required for efficient capping, splicing, and cleavage/polyadenylation of pre-mRNAs (15,29,47). In fact, the CTD has been described as a platform that recruits RNA processing/ export and histone-modifying factors to the transcription complex, coupling mRNA metabolism to chromatin function (8, 54).The CTD is characterized by repetition of the consensus heptapeptide sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser, ranging from 26 repeats in yeast to 52 in mammals, which is subjected to highly regulated phosphorylation (14,15,47). Unphosphorylated RNAP II is mostly recruited to the preinitiation complex (PIC) (45), and hyperphosphorylated RNAP II is associated with initiation and elongation complexes (42). The CTD is phosphorylated on serine 5 of the heptapeptide repeat predominantly during promoter escape and early elongation, while serine 2 becomes phosphorylated principally during elongation (16,38). In addition, it has recently been demonstrated that the CTD can be also phosphorylated on serine 7 (3, 13, 25

show abstract

Phosphorylation by Cak1 Regulates the C-Terminal Domain Kinase Ctk1 in Saccharomyces cerevisiae

Cited by 29 publications

References 43 publications

Sister Chromatid Cohesion Role for CDC28-CDK in Saccharomyces cerevisiae

Sister Chromatid Cohesion Role for CDC28-CDK in Saccharomyces cerevisiae

Ascospore Formation in the YeastSaccharomyces cerevisiae

Sub1 Globally Regulates RNA Polymerase II C-Terminal Domain Phosphorylation

Contact Info

Product

Resources

About