Prospore membrane formation linked to the leading edge protein (LEP) coat assembly

Moreno‐Borchart, Alexandra C.; Strasser, Katrin; Finkbeiner, Martin G.; Shevchenko, Anna; Shevchenko, Andrej; Knop, Michael

doi:10.1093/emboj/20.24.6946

Cited by 60 publications

(131 citation statements)

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“…Immunofluorescence and electron microscopy of sporulating yeast cells have been described previously (Moreno-Borchart et al, 2001). …”

Section: Immunofluorescence and Electron Microscopymentioning

confidence: 99%

“…Anti-Sec9p-CT antibodies have been described previously (Brennwald et al, 1994). AntiSec4p (R232), Sec15p (R233), Sso1/2p (K8), Sso1p (K6916), Sso2p (K6906), Mso1p (R285), tubulin, and Ady3p antibodies have been described previously (Aalto et al, 1997;Moreno-Borchart et al, 2001;Jantti et al, 2002;Toikkanen et al, 2003). Anti-Sec8p antibody was obtained from Wei Guo (University of Pennsylvania, Philadelphia, PA).…”

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confidence: 99%

“…Based on the 4,6-diamidino-2-phenylindole (DAPI) labeling, MSO1 deletion did not impair entry into and progression through the meiotic divisions (our unpublished data). However, analysis of different stages of PSM assembly, by using Ady3p as a marker for prospore membrane (Moreno-Borchart et al, 2001), revealed that prospore membranes did not assemble in the ⌬mso1 mutant and that the Ady3p marker localized to clusters at the meiotic SPBs ( Figure 1A). The phenotype was reminiscent to the one observed in the ⌬mpc54 ⌬mpc70 mutant.…”

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confidence: 99%

“…Faint staining was visible all along the extended prospore membranes throughout the growth of the membranes during anaphase of meiosis II ( Figure 2B, top, metaphase; bottom, anaphase). Ady3p was visualized by immunofluorescence to detect the leading edge of the growing prospore membranes (Moreno-Borchart et al, 2001). Previously, Sec1p has been localized by GFP tagging to a restricted area in the bud and in the neck region of dividing vegetatively grown mitotic cells (Carr et al, 1999).…”

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Molecular Interactions Position Mso1p, a Novel PTB Domain Homologue, in the Interface of the Exocyst Complex and the Exocytic SNARE Machinery in Yeast

Knop

Miller

Mazza

et al. 2005

MBoC

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In this study, we have analyzed the association of the Sec1p interacting protein Mso1p with the membrane fusion machinery in yeast. We show that Mso1p is essential for vesicle fusion during prospore membrane formation. Green fluorescent protein-tagged Mso1p localizes to the sites of exocytosis and at the site of prospore membrane formation. In vivo and in vitro experiments identified a short amino-terminal sequence in Mso1p that mediates its interaction with Sec1p and is needed for vesicle fusion. A point mutation, T47A, within the Sec1p-binding domain abolishes Mso1p functionality in vivo, and mso1T47A mutant cells display specific genetic interactions with sec1 mutants. Mso1p coimmunoprecipitates with Sec1p, Sso1/2p, Snc1/2p, Sec9p, and the exocyst complex subunit Sec15p. In sec4-8 and SEC4I133 mutant cells, association of Mso1p with Sso1/2p, Snc1/2p, and Sec9p is affected, whereas interaction with Sec1p persists. Furthermore, in SEC4I133 cells the dominant negative Sec4I133p coimmunoprecipitates with Mso1p-Sec1p complex. Finally, we identify Mso1p as a homologue of the PTB binding domain of the mammalian Sec1p binding Mint proteins.These results position Mso1p in the interface of the exocyst complex, Sec4p, and the SNARE machinery, and reveal a novel layer of molecular conservation in the exocytosis machinery. INTRODUCTIONEvolutionarily conserved molecular machinery regulates transport vesicle targeting, tethering, and fusion in eukaryotic cells. In yeast Saccharomyces cerevisiae this machinery involves the activity of the eight-subunit (Sec3p, Sec5p, Sec6p, Sec8p, Sec10p, Sec15p, Exo70p, and Exo84p) tethering complex, the exocyst, a rab family small GTPase Sec4p, and the exocytic SNARE complex (Snc1/2p, Sec9p, and Sso1/2p) thought to drive the actual lipid bilayer fusion . The exocyst subunit Sec15p has been shown to act as an effector for Sec4p (Guo et al., 1999). In addition, sec4-8 mutant cells are defective in Snc1/2p-Sec9p-Sso1/2p SNARE complex assembly (Carr et al., 1999). Despite these and numerous other studies, the regulatory mechanisms for SNARE complex formation are still poorly understood. The Sec1/Munc18 (SM) protein family members represent central regulators of SNARE complex function. These proteins perform an essential, albeit currently poorly understood function in SNARE complex regulation (Gallwitz and Jahn, 2003;Toonen and Verhage, 2003;Kauppi et al., 2004).Yeast S. cerevisiae possesses four Sec1p-family proteins: Sec1p mediates vesicle fusion at the plasma membrane (Novick et al., 1981;Carr et al., 1999), Sly1p mediates vesicle fusion at the endoplasmic reticulum-Golgi interface (Ossig et al., 1991), Vps33p is required for endosome to vacuole transport and vacuole maintenance (Banta et al., 1990), and Vps45p mediates Golgi-to-vacuole transport (Piper et al., 1994;Cowles et al., 1994). Sec1p is the closest homologue of the mammalian Munc18-1 that has been shown to associate with syntaxin 1 and to regulate the syntaxin 1-synaptobrevin-SNAP-25 SNARE complex assembly (Misura et al., 2000;Kaup...

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“…Immunofluorescence and electron microscopy of sporulating yeast cells have been described previously (Moreno-Borchart et al, 2001). …”

Section: Immunofluorescence and Electron Microscopymentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Molecular Interactions Position Mso1p, a Novel PTB Domain Homologue, in the Interface of the Exocyst Complex and the Exocytic SNARE Machinery in Yeast

Knop

Miller

Mazza

et al. 2005

MBoC

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“…Expansion of the PSM depends on a complex of proteins, called the leading-edge complex, which includes Don1, Ssp1, and Ady3 (Moreno-Borchart et al 2001;Nickas and Neiman 2002). These proteins initially localize to the SPB; as the PSM expands to engulf the adjacent nucleus, they localize to a ring corresponding to the growing edge of the PSM.…”

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SSP2 and OSW1, Two Sporulation-Specific Genes Involved in Spore Morphogenesis in Saccharomyces cerevisiae

Agarwal

Roeder

2007

Genetics

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Spore formation in Saccharomyces cerevisiae requires the synthesis of prospore membranes (PSMs) followed by the assembly of spore walls (SWs). We have characterized extensively the phenotypes of mutants in the sporulation-specific genes, SSP2 and OSW1, which are required for spore formation. A striking feature of the osw1 phenotype is asynchrony of spore development, with some spores displaying defects in PSM formation and others spores in the same ascus blocked at various stages in SW development. The Osw1 protein localizes to spindle pole bodies (SPBs) during meiotic nuclear division and subsequently to PSMs/SWs. We propose that Osw1 performs a regulatory function required to coordinate the different stages of spore morphogenesis. In the ssp2 mutant, nuclei are surrounded by PSMs and SWs; however, PSMs and SWs often also encapsulate anucleate bodies both inside and outside of spores. In addition, the SW is not as thick as in wild type. The ssp2 mutant defect is partially suppressed by overproduction of either Spo14 or Sso1, both of which promote the fusion of vesicles at the outer plaque of the SPB early in PSM formation. We propose that Ssp2 plays a role in vesicle fusion during PSM formation.S PORULATION in the budding yeast, Saccharomyces cerevisiae, involves two overlapping processesmeiosis and spore morphogenesis. During meiosis, a diploid cell undergoes a single round of DNA replication, followed by two rounds of chromosome segregation, to generate four haploid nuclei. During spore morphogenesis, the four daughter nuclei are packaged into spores, which are contained within an ascus.Spore morphogenesis (reviewed by Neiman 2005) initiates with enlargement of the outer surface of the spindle pole body (SPB) to form the meiotic outer plaque. As cells undergo meiosis II, vesicles coalesce on the meiotic plaque to form a novel intracellular membrane called the prospore membrane (PSM). The doublelayered PSM extends outward from each SPB to surround the adjacent nucleus. When the leading edges of the PSM meet and become fused, the haploid nucleus is fully encapsulated to form a prospore. PSM closure triggers the final step of spore morphogenesis, spore wall (SW) formation. The SW is assembled between the two membranes of the PSM and consists of four layers. The two inner layers are composed of glucan and mannan, which are components of vegetative cell walls.

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Asymmetric Segregation of Age‐Induced Damage in Budding Yeast

Goodman

Ünal

2020

Encyclopedia of Life Sciences

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Cellular damage follows an asymmetric pattern of inheritance in budding yeast. Age‐associated factors accrue in mother cells after each mitotic division, while the ensuing daughter cells are devoid of any damage. Mother cells retain dysfunctional organelles, including oxidised mitochondria, alkaline vacuoles and a nucleus with a weakened permeability barrier. The nucleus of the mother cell contains additional ageing factors such as misfolded proteins, ribosomal DNA (rDNA) circles and fragmented nucleoli. These factors persist throughout replicative ageing and may contribute to cellular senescence. Interestingly, protein aggregates and nucleolar aberrations retained in mitosis are excluded from the meiotic products, also known as gametes. This occurs by a five‐way nuclear division during meiosis II, where the genetic material destined for four gametes is physically separated away from the age‐induced damage through the formation of a fifth nuclear compartment, which eventually gets degraded during gamete maturation. As a result of this specialised nuclear division, meiotic progeny is born young, devoid of any preexisting damage. Key Concepts Age‐induced damage is asymmetrically retained in mother cells during mitosis. Organelle function declines in mother cells as they undergo replicative aging. A diffusion barrier at the bud neck, the region between the mother and daughter cell, facilitates the retention of nuclear and endoplasmic reticulum (ER) age‐induced damage. Age‐induced damage from mother cells is not passed onto the meiotic products. Gametes generated by old mother cells are rejuvenated and have the same replicative lifespan as gametes generated by young mother cells.

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Prospore membrane formation linked to the leading edge protein (LEP) coat assembly

Cited by 60 publications

References 51 publications

Molecular Interactions Position Mso1p, a Novel PTB Domain Homologue, in the Interface of the Exocyst Complex and the Exocytic SNARE Machinery in Yeast

Molecular Interactions Position Mso1p, a Novel PTB Domain Homologue, in the Interface of the Exocyst Complex and the Exocytic SNARE Machinery in Yeast

SSP2 and OSW1, Two Sporulation-Specific Genes Involved in Spore Morphogenesis in Saccharomyces cerevisiae

Asymmetric Segregation of Age‐Induced Damage in Budding Yeast

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