title: Mutational analysis of essential septins reveals a role for septin-mediated signaling in filamentation.
abstract: Septin proteins are conserved structural proteins that often demarcate regions of cell division. The essential nature of the septin ring, composed of several septin proteins, complicates investigation of the functions of the ring, although careful analysis in the model yeast Saccharomyces cerevisiae has elucidated the role that septins play in the cell cycle. Mutation analysis of nonessential septins in the pathogenic fungus Candida albicans has shown that septins also have vital roles in cell wall regulation (CWR), hyphal formation, and pathogenesis. While mutations in nonessential septins have been useful in establishing phenotypes, the septin defect is so slight that identifying causative associations between septins and downstream effectors has been difficult. In this work, we describe decreased abundance by mRNA perturbation (DAmP) alleles of essential septins, which display a septin defect more severe than the defect observed in deletions of nonessential septins. The septin DAmP alleles have allowed us to genetically separate the roles of septins in hyphal growth and CWR and to identify the cyclic AMP pathway as a pathway that likely acts in a parallel manner with septins in hyphal morphogenesis.
authors.affiliation: Department of Biology, University of Nebraska Omaha, Omaha, Nebraska, USA Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA jrblankenship@unomaha.edu.
authors.forename: Jill R
authors.initials: JR
authors.lastname: Blankenship
authors.affiliation: Department of Medicine, Infectious Disease Division, University of Pittsburgh Medical Center, Pittsburgh, Pennsylvania, USA.
authors.forename: Shaoji
authors.initials: S
authors.lastname: Cheng
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA.
authors.forename: Carol A
authors.initials: CA
authors.lastname: Woolford
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA.
authors.forename: Wenjie
authors.initials: W
authors.lastname: Xu
authors.affiliation: Department of Biology, University of Nebraska Omaha, Omaha, Nebraska, USA.
authors.forename: Tanner M
authors.initials: TM
authors.lastname: Johnson
authors.affiliation: Department of Clinical Pharmacy, College of Pharmacy, University of Tennessee Health Science Center, Memphis, Tennessee, USA.
authors.forename: P David
authors.initials: PD
authors.lastname: Rogers
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA.
authors.forename: Saranna
authors.initials: S
authors.lastname: Fanning
authors.affiliation: Department of Medicine, Infectious Disease Division, University of Pittsburgh Medical Center, Pittsburgh, Pennsylvania, USA.
authors.forename: M Hong
authors.initials: MH
authors.lastname: Nguyen
authors.affiliation: Department of Medicine, Infectious Disease Division, University of Pittsburgh Medical Center, Pittsburgh, Pennsylvania, USA.
authors.forename: Cornelius J
authors.initials: CJ
authors.lastname: Clancy
authors.affiliation: Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania, USA.
authors.forename: Aaron P
authors.initials: AP
authors.lastname: Mitchell
mesh_terms: D000818:Animals; D002176:Candida albicans / Q000235:genetics* / Q000472:pathogenicity; D002177:Candidiasis / Q000235:genetics / Q000473:pathology; D018797:Cell Cycle Proteins / Q000235:genetics; D002455:Cell Division / Q000235:genetics; D002473:Cell Wall / Q000235:genetics; D017868:Cyclic AMP-Dependent Protein Kinases / Q000096:biosynthesis / Q000235:genetics; D003599:Cytoskeleton / Q000235:genetics; D004252:DNA Mutational Analysis; D004268:DNA-Binding Proteins / Q000096:biosynthesis; D005656:Fungal Proteins / Q000096:biosynthesis; D025301:Hyphae / Q000235:genetics* / Q000254:growth & development*; D008297:Male; D051379:Mice; D008813:Mice, Inbred ICR; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis / Q000235:genetics; D058112:Septins / Q000235:genetics*; D015398:Signal Transduction / Q000235:genetics; D014157:Transcription Factors / Q000096:biosynthesis
chemical_list: D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; C121438:EFG1 protein, Candida albicans; D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D017868:Cyclic AMP-Dependent Protein Kinases; C579078:Tpk1 protein, S cerevisiae; D058112:Septins