title: Regulation of Sphingolipid Biosynthesis by the Morphogenesis Checkpoint Kinase Swe1.
abstract: Sphingolipid (SL) biosynthesis is negatively regulated by the highly conserved endoplasmic reticulum-localized Orm family proteins. Defective SL synthesis in Saccharomyces cerevisiae leads to increased phosphorylation and inhibition of Orm proteins by the kinase Ypk1. Here we present evidence that the yeast morphogenesis checkpoint kinase, Swe1, regulates SL biosynthesis independent of the Ypk1 pathway. Deletion of the Swe1 kinase renders mutant cells sensitive to serine palmitoyltransferase inhibition due to impaired sphingoid long-chain base synthesis. Based on these data and previous results, we suggest that Swe1 kinase perceives alterations in SL homeostasis, activates SL synthesis, and may thus represent the missing regulatory link that controls the SL rheostat during the cell cycle.
authors.affiliation: From the Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, Humboldtstrasse 50/II, 8010 Graz, Austria and.
authors.forename: Neha
authors.initials: N
authors.lastname: Chauhan
authors.affiliation: the Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814.
authors.forename: Gongshe
authors.initials: G
authors.lastname: Han
authors.affiliation: the Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814.
authors.forename: Niranjanakumari
authors.initials: N
authors.lastname: Somashekarappa
authors.affiliation: the Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814.
authors.forename: Kenneth
authors.initials: K
authors.lastname: Gable
authors.affiliation: the Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814 teresa.dunn-giroux@usuhs.edu.
authors.forename: Teresa
authors.initials: T
authors.lastname: Dunn
authors.affiliation: From the Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, Humboldtstrasse 50/II, 8010 Graz, Austria and sepp.kohlwein@uni-graz.at.
authors.forename: Sepp D
authors.initials: SD
authors.lastname: Kohlwein
mesh_terms: D018797:Cell Cycle Proteins / Q000378:metabolism*; D002455:Cell Division; D005229:Fatty Acids, Monounsaturated / Q000737:chemistry; D015966:Gene Expression Regulation, Fungal; D005982:Glutathione Transferase / Q000378:metabolism; D038362:Glycogen Synthase Kinase 3 / Q000378:metabolism; D006706:Homeostasis; D009154:Mutation; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D051102:Serine C-Palmitoyltransferase; D013107:Sphingolipids / Q000096:biosynthesis*
chemical_list: D018797:Cell Cycle Proteins; D005229:Fatty Acids, Monounsaturated; C548540:Orm2 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013107:Sphingolipids; D051102:Serine C-Palmitoyltransferase; D005982:Glutathione Transferase; C099685:SWE1 protein, S cerevisiae; D011505:Protein-Tyrosine Kinases; D038362:Glycogen Synthase Kinase 3; C068124:MCK1 protein, S cerevisiae; C001996:thermozymocidin
keywords: cell cycle; metabolic regulation; phosphorylation; serine palmitoyltransferase; sphingolipid; yeast