Identification of a developmentally regulated septin and involvement of the septins in spore formation in Saccharomyces cerevisiae.

Fares, Hanna; Goetsch, Loretta; Pringle, John R.

doi:10.1083/jcb.132.3.399

Cited by 166 publications

(187 citation statements)

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“…SPR3 and SPR28 encode sporulation-specific septins most closely related to CDC12 and CDC11, respectively, that are induced as middle genes (Holaway et al 1987;Ozsarac et al 1995;De Virgilio et al 1996;Fares et al 1996). Interestingly, the vegetative septins CDC3 and CDC10 are also transcriptionally upregulated during sporulation, while CDC12, CDC11, and SHS1 are not (Kaback and Feldberg 1985;.…”

Section: Membrane-cytoskeletal Interactionsmentioning

confidence: 99%

Sporulation in the Budding Yeast Saccharomyces cerevisiae

2011

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In response to nitrogen starvation in the presence of a poor carbon source, diploid cells of the yeast Saccharomyces cerevisiae undergo meiosis and package the haploid nuclei produced in meiosis into spores. The formation of spores requires an unusual cell division event in which daughter cells are formed within the cytoplasm of the mother cell. This process involves the de novo generation of two different cellular structures: novel membrane compartments within the cell cytoplasm that give rise to the spore plasma membrane and an extensive spore wall that protects the spore from environmental insults. This article summarizes what is known about the molecular mechanisms controlling spore assembly with particular attention to how constitutive cellular functions are modified to create novel behaviors during this developmental process. Key regulatory points on the sporulation pathway are also discussed as well as the possible role of sporulation in the natural ecology of S. cerevisiae. TABLE OF CONTENTS Abstract 737Introduction 738

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Section: Membrane-cytoskeletal Interactionsmentioning

confidence: 99%

Sporulation in the Budding Yeast Saccharomyces cerevisiae

2011

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“…In mitotic cells, these septins are implicated in bud-site selection, the establishment and maintenance of polarized bud growth, the switch from polarized to isotropic bud growth, and spindle positioning [14][15][16]. In meiotic cells, two sporulation-specific septins (Spr3 and Spr28) replace Cdc12 and Shs1, respectively, and form an alternative complex with Cdc3, Cdc10 and Cdc11 that localizes to the prospore envelope as it forms [17,18]. In fission yeast, septins Spn1, Spn2, Spn3 and Spn4, which are homologous to Cdc3, Cdc10, Cdc11 and Cdc12, respectively (Table 1), colocalize at the medial cortex (See Glossary) as a double-ring structure at the onset of cytokinesis.…”

Section: Septin Functionsmentioning

confidence: 99%

Some assembly required: yeast septins provide the instruction manual

Versele

Thorner

2005

Trends in Cell Biology

201

199

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Septins are a family of conserved proteins that form hetero-oligomeric complexes that assemble into filaments. The filaments can be organized into linear arrays, coils, rings and gauzes. They serve as membrane-associated scaffolds and as barriers to demarcate local compartments, especially for the establishment of the septation site for cytokinesis. Studies in budding and fission yeast have revealed many of the protein-protein interactions that govern the formation of multi-septin complexes. GTP binding and phosphorylation direct the polymerization of filaments that is required for septin-collar assembly in budding yeast, whereas a homolog of anillin instructs timely formation of the ring of septin filaments at the medial cortex in fission yeast. These insights should aid understanding of the organization and function of the diverse septin structures in animal cells.

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“…In Saccharomyces cerevisiae, there are seven septin genes, of which five (CDC3, CDC10, CDC11, CDC12, and SHS1/SEP7) are expressed in vegetative cells (Longtine et al, 1996;Carroll et al, 1998;Mino et al, 1998) and two (SPR3 and SPR28) only during sporulation (DeVirgilio et al, 1996;Fares et al, 1996). The five vegetatively expressed septins have identical localization patterns throughout the cell cycle.…”

Section: Introductionmentioning

confidence: 99%

“…In each species examined to date, there are two or more septins that form heterooligomeric complexes to perform their specific functions. Purified septins from yeast, Drosophila, Xenopus, and mammalian cells form filaments of 7-9 nm diameter and of variable length (Field et al, 1996;Frazier et al, 1998;Hsu et al, 1998;Kinoshita et al, 2002;Mendoza et al, 2002).In Saccharomyces cerevisiae, there are seven septin genes, of which five (CDC3, CDC10, CDC11, CDC12, and SHS1/SEP7) are expressed in vegetative cells (Longtine et al, 1996;Carroll et al, 1998;Mino et al, 1998) and two (SPR3 and SPR28) only during sporulation (DeVirgilio et al, 1996;Fares et al, 1996). The five vegetatively expressed septins have identical localization patterns throughout the cell cycle.…”

mentioning

confidence: 99%

The Role of Cdc42p GTPase-activating Proteins in Assembly of the Septin Ring in Yeast

Caviston

Longtine

Pringle

et al. 2003

MBoC

228

281

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The septins are a conserved family of GTP-binding, filament-forming proteins. In the yeast Saccharomyces cerevisiae, the septins form a ring at the mother-bud neck that appears to function primarily by serving as a scaffold for the recruitment of other proteins to the neck, where they participate in cytokinesis and a variety of other processes. Formation of the septin ring depends on the Rho-type GTPase Cdc42p but appears to be independent of the actin cytoskeleton. In this study, we investigated further the mechanisms of septin-ring formation. Fluorescence-recovery-after-photobleaching (FRAP) experiments indicated that the initial septin structure at the presumptive bud site is labile (exchanges subunits freely) but that it is converted into a stable ring as the bud emerges. Mutants carrying the cdc42 V36G allele or lacking two or all three of the known Cdc42p GTPase-activating proteins (GAPs: Bem3p, Rga1p, and Rga2p) could recruit the septins to the cell cortex but were blocked or delayed in forming a normal septin ring and had accompanying morphogenetic defects. These phenotypes were dramatically enhanced in mutants that were also defective in Cla4p or Gin4p, two protein kinases previously shown to be important for normal septin-ring formation. The Cdc42p GAPs colocalized with the septins both early and late in the cell cycle, and overexpression of the GAPs could suppress the septin-organization and morphogenetic defects of temperature-sensitive septin mutants. Taken together, the data suggest that formation of the mature septin ring is a process that consists of at least two distinguishable steps, recruitment of the septin proteins to the presumptive bud site and their assembly into the stable septin ring. Both steps appear to depend on Cdc42p, whereas the Cdc42p GAPs and the other proteins known to promote normal septin-ring formation appear to function in a partially redundant manner in the assembly step. In addition, because the eventual formation of a normal septin ring in a cdc42 V36G or GAP mutant was invariably accompanied by a switch from an abnormally elongated to a more normal bud morphology distal to the ring, it appears that the septin ring plays a direct role in determining the pattern of bud growth. INTRODUCTIONThe septin family of proteins was first recognized in yeast and now appears to be ubiquitous in fungi and animals, although not in plants (Longtine et al., 1996;Field and Kellogg, 1999;Trimble, 1999;Nguyen et al., 2000;Momany et al., 2001;Macara et al., 2002). Typical septins have a variable N-terminal region, a conserved core that includes the elements of a GTP-binding site, and a variable C-terminal region that (in all but a few cases) includes a predicted coiled-coil domain. In each species examined to date, there are two or more septins that form heterooligomeric complexes to perform their specific functions. Purified septins from yeast, Drosophila, Xenopus, and mammalian cells form filaments of 7-9 nm diameter and of variable length (Field et al., 1996;Frazier et al., 1998;Hsu et al...

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Identification of a developmentally regulated septin and involvement of the septins in spore formation in Saccharomyces cerevisiae.

Cited by 166 publications

References 84 publications

Sporulation in the Budding Yeast Saccharomyces cerevisiae

Sporulation in the Budding Yeast Saccharomyces cerevisiae

Some assembly required: yeast septins provide the instruction manual

The Role of Cdc42p GTPase-activating Proteins in Assembly of the Septin Ring in Yeast

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