Role of the spindle pole body of yeast in mediating assembly of the prospore membrane during meiosis

Knop, Michael; Strasser, Katrin

doi:10.1093/emboj/19.14.3657

Cited by 112 publications

(249 citation statements)

References 43 publications

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“…In MSO1-deleted cells (⌬mso1), no prospore formation occurred, but instead numerous 60-to 70-nm vesicles accumulated at the SPB ( Figure 1B). These vesicle were frequently seen lined along the cytoplasmic side of the SPB, which at this stage of meiosis is modified with the meiotic plaque composed of Mpc54p, Mpc70p, and Spo74p (Knop and Strasser, 2000;Nickas and Neiman, 2002). This indicates that these vesicles have been docked to the scaffold of the meiotic SPB, but they seem to have failed to fuse and form a prospore membrane.…”

Section: Mso1p Is Essential For Membrane Fusion During Prospore Membrmentioning

confidence: 99%

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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Section: Mso1p Is Essential For Membrane Fusion During Prospore Membrmentioning

confidence: 99%

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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Section: Key Events In the Phases Of Sporulationmentioning

confidence: 99%

“…At meiosis II, Spc72 disappears (presumably by proteolysis) and several sporulation-specific proteins are recruited to form a greatly expanded cytoplasmic face termed the meiosis II outer plaque (MOP) (Moens and Rapport 1971;Knop and Strasser 2000) (Figure 2). The major MOP proteins are Spo21/Mpc70, Mpc54, and Spo74 (Knop and Strasser 2000;Bajgier et al 2001;Nickas et al 2003). The constitutive SPB proteins Cnm67 and Nud1 are also present in the MOP, as is Ady4, a minor component important for MOP complex stability (Knop and Strasser 2000;Nickas et al 2003;Mathieson et al 2010a).…”

Section: Key Events In the Phases Of Sporulationmentioning

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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“…By electron microscopy, the leading edge of FSM is observed as an electron dense structure, which is apparently distinct from the FSM (Hirata, unpublished data). Several proteins have been identified as leading edge components both in S. cerevisiae and S. pombe (Knop and Strasser, 2000;MorenoBorchart et al, 2001;Nickas and Neiman, 2002;Okuzaki et al, 2003;Itadani et al, 2006). In S. pombe, Meu14 is one of the leading edge components.…”

Section: Closure Of the Fsmmentioning

confidence: 99%

Live Observation of Forespore Membrane Formation in Fission Yeast

Nakamura

Asakawa

Nakase

et al. 2008

MBoC

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Sporulation in the fission yeast Schizosaccharomyces pombe is a unique biological process in that the plasma membrane of daughter cells is assembled de novo within the mother cell cytoplasm. A double unit membrane called the forespore membrane (FSM) is constructed dynamically during meiosis. To obtain a dynamic view of FSM formation, we visualized FSM in living cells by using green fluorescent protein fused with Psy1, an FSM-resident protein, together with the nucleus or microtubules. The assembly of FSM initiates in prophase II, and four FSMs in a cell expand in a synchronous manner at the same rate throughout meiosis II. After the meiosis II completes, FSMs continue to expand until closure to form the prespore, a spore precursor. Prespores are initially ellipsoidal, and eventually become spheres. FSM formation was also observed in the sporulation-deficient mutants spo3, spo14, and spo15. In the spo15 mutant, the initiation of FSM formation was completely blocked. In the spo3 mutant, the FSM expanded normally during early meiosis II, but it was severely inhibited during late and postmeiosis, whereas in the spo14 mutant, membrane expansion was more severely inhibited throughout meiosis II. These observations suggest that FSM expansion is composed of two steps, early meiotic FSM expansion and late and post meiotic FSM expansion. Possible regulatory mechanisms of FSM formation in fission yeast are discussed.

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Role of the spindle pole body of yeast in mediating assembly of the prospore membrane during meiosis

Cited by 112 publications

References 43 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

Sporulation in the Budding Yeast Saccharomyces cerevisiae

Live Observation of Forespore Membrane Formation in Fission Yeast

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