title: Prenylated isoforms of yeast casein kinase I, including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase.
abstract: The GCS1 gene of the budding yeast Saccharomyces cerevisiae mediate the resumption of cell proliferation from the starved, stationary-phase state. Here we identify yeast genes that, in increased dosages, overcome the growth defect of gcs1 delta mutant cells. Among these are YCK1 (CK12) and YCK2 (CKI1), encoding membrane-associated casein kinase I, and YCK3, encoding a novel casein kinase I isoform. Some Yck3p gene product was found associated with the plasma membrane, like Yck1p and Yck2p, but most confractionated with the nucleus, like another yeast casein kinase I isoform, Hrr25p. Genetic studies showed that YCK3 and HRR25 constitute an essential gene family and that Yck3p can weakly substitute for Yck1p-Yck2p. For gcs1 delta suppression, both a protein kinase domain and a C-terminal prenylation motif were shown to be necessary. An impairment in endocytosis was found for gcs1 delta mutant cells, which was alleviated by an increased YCK2 gene dosage. The ability of an increased casein kinase I gene dosage to suppress the effects caused by the absence of Gcs1p suggests that Gcs1p and Yck1p-Yck2p affect parallel pathways.
authors.affiliation: Department of Biochemistry, Dalhousie University, Halifax, Nova Scotia, Canada.
authors.forename: X
authors.initials: X
authors.lastname: Wang
authors.forename: M F
authors.initials: MF
authors.lastname: Hoekstra
authors.forename: A J
authors.initials: AJ
authors.lastname: DeMaggio
authors.forename: N
authors.initials: N
authors.lastname: Dhillon
authors.forename: A
authors.initials: A
authors.lastname: Vancura
authors.forename: J
authors.initials: J
authors.lastname: Kuret
authors.forename: G C
authors.initials: GC
authors.lastname: Johnston
authors.forename: R A
authors.initials: RA
authors.lastname: Singer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D047389:Casein Kinase I; D047388:Casein Kinases; D002417:Cattle; D002453:Cell Cycle; D002455:Cell Division; D005800:Genes, Fungal; D005838:Genotype; D007527:Isoenzymes / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D008961:Models, Structural; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D017368:Protein Prenylation; D017433:Protein Structure, Secondary; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000254:growth & development / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D013489:Suppression, Genetic
chemical_list: D007527:Isoenzymes; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases; D047389:Casein Kinase I; D047388:Casein Kinases; C479664:YCK1 protein, S cerevisiae; C479666:YCK2 protein, S cerevisiae; D011493:Protein Kinase C