Vesicle Docking to the Spindle Pole Body Is Necessary to Recruit the Exocyst During Membrane Formation in<i>Saccharomyces cerevisiae</i>

Mathieson, Erin M.; Suda, Yuji; Nickas, Mark E.; Snydsman, Brian E.; Davis, Trisha N.; Muller, Eric G D; Neiman, Aaron M.

doi:10.1091/mbc.e10-07-0563

Cited by 22 publications

(24 citation statements)

References 52 publications

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“…Similarly, the MOP proteins Spo21 and Mpc54 are also predicted coiled-coil proteins and fluorescence resonance energy transfer studies suggest that they are arranged with their N termini out toward the cytoplasm and their C termini inward (Mathieson et al 2010b) (Figure 2A). The C termini are located near the N terminus of Cnm67, which links the MOP to the central domain of the SPB (Schaerer et al 2001) (Figure 2).…”

Section: Key Events In the Phases Of Sporulationmentioning

confidence: 88%

“…Fusion of additional vesicles then expands the prospore membrane beyond the MOP ( Figure 3D). Mutations in conserved residues in the N-terminal (membraneproximal) domain of Mpc54 cause a defect in which vesicles associate with the MOP but do not dock stably onto its surface (Mathieson et al 2010b). These undocked, MOPassociated vesicles do not fuse with each other.…”

Section: Key Events In the Phases Of Sporulationmentioning

confidence: 99%

“…Thus, docking of the vesicles to the MOP is an essential prerequisite to their fusion. Furthermore, the Rab family GTPase Sec4, as well as several components of the exocyst complex, are present on vesicles when they are docked to the MOP but absent from the MOP-associated vesicles in the mpc54 point mutants (Mathieson et al 2010b). These observations suggest that the MOP controls the formation of prospore membranes in two ways.…”

Section: Key Events In the Phases Of Sporulationmentioning

confidence: 99%

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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: Key Events In the Phases Of Sporulationmentioning

confidence: 88%

Section: Key Events In the Phases Of Sporulationmentioning

confidence: 99%

Section: Key Events In the Phases Of Sporulationmentioning

confidence: 99%

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Sporulation in the Budding Yeast Saccharomyces cerevisiae

2011

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“…RHO1 also plays an important role in membrane fusion by serving as an anchor for SEC3 (32,33), a component of the hetero-octameric exocyst protein complex. Three of the eight exocyst subunits were quantified from the nanoLC-FAIMS-MS experiments whereas none were identified from the nanoLC-MS experiments.…”

Section: Nanolc-faims-ms Of a Complexmentioning

confidence: 99%

Nanospray FAIMS Fractionation Provides Significant Increases in Proteome Coverage of Unfractionated Complex Protein Digests

Swearingen

Hoopmann

Johnson

et al. 2012

Molecular & Cellular Proteomics

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High-field asymmetric waveform ion mobility spectrometry (FAIMS) is an atmospheric pressure ion mobility technique that can be used to reduce sample complexity and increase dynamic range in tandem mass spectrometry experiments. FAIMS fractionates ions in the gas-phase according to characteristic differences in mobilities in electric fields of different strengths. Undesired ion species such as solvated clusters and singly charged chemical background ions can be prevented from reaching the mass analyzer, thus decreasing chemical noise. To date, there has been limited success using the commercially available Thermo Fisher FAIMS device with both standard ESI and nanoLC-MS. We have modified a Thermo Fisher electrospray source to accommodate a fused silica pulled tip capillary column for nanospray ionization, which will enable standard laboratories access to FAIMS technology. Our modified source allows easily obtainable stable spray at flow rates of 300 nL/min when coupled with FAIMS. The modified electrospray source allows the use of sheath gas, which provides a fivefold increase in signal obtained when nanoLC is coupled to FAIMS. In this work, nanoLC-FAIMS-MS and nanoLC-MS were compared by analyzing a tryptic digest of a 1:1 mixture of SILAC-labeled haploid and diploid yeast to demonstrate the performance of nanoLC-FAIMS-MS, at different compensation voltages, for post-column fractionation of complex protein digests. The effective dynamic range more than doubled when FAIMS was used. In total, 10,377 unique stripped peptides and 1649 unique proteins with SILAC ratios were identified from the combined nanoLC-FAIMS-MS experiments, compared with 6908 unique stripped peptides and 1003 unique proteins with SILAC ratios identified from the combined nanoLC-MS ex-

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“…Fluorescent proteins linked to these ends were later directly visualized at the predicted locations via electron microscopy (67). FRET R has also been used to analyze the structure of the yeast spindle pole body (24,68) and cohesion architecture (69), and more recently the organization of the yeast kinetochore (26). Of course FRET R also has limitations, and it is most appropriate for experimental conditions in which the proteins in a complex are uniformly tagged with a fluorescent protein, gene expression is tightly regulated and typically driven from native promoters, and free unincorporated proteins do not interfere with the FRET measurements (17,(23)(24)(25).…”

Section: Resultsmentioning

confidence: 99%

Determining Protein Complex Structures Based on a Bayesian Model of in Vivo Förster Resonance Energy Transfer (FRET) Data

Bonomi

Pellarin

Kim

et al. 2014

Molecular & Cellular Proteomics

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The use of in vivo Fö rster resonance energy transfer (FRET) data to determine the molecular architecture of a protein complex in living cells is challenging due to data sparseness, sample heterogeneity, signal contributions from multiple donors and acceptors, unequal fluorophore brightness, photobleaching, flexibility of the linker connecting the fluorophore to the tagged protein, and spectral cross-talk. We addressed these challenges by using a Bayesian approach that produces the posterior probability of a model, given the input data. The posterior probability is defined as a function of the dependence of our FRET metric FRET R on a structure (forward model), a model of noise in the data, as well as prior information about the structure, relative populations of distinct states in the sample, forward model parameters, and data noise. The forward model was validated against kinetic Monte Carlo simulations and in vivo experimental data collected on nine systems of known structure. In addition, our Bayesian approach was validated by a benchmark of 16 protein complexes of known structure. Given the structures of each subunit of the complexes, models were computed from synthetic FRET R data with a distance root-mean-squared deviation error of 14 to 17 Å . The approach is implemented in the open-source Integrative Modeling Platform, allowing us to determine macromolecular structures through a combination of in vivo FRET R data and data from other sources, such as electron microscopy and chemical cross-linking. Molecular & Cellular

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Vesicle Docking to the Spindle Pole Body Is Necessary to Recruit the Exocyst During Membrane Formation inSaccharomyces cerevisiae

Cited by 22 publications

References 52 publications

Sporulation in the Budding Yeast Saccharomyces cerevisiae

Sporulation in the Budding Yeast Saccharomyces cerevisiae

Nanospray FAIMS Fractionation Provides Significant Increases in Proteome Coverage of Unfractionated Complex Protein Digests

Determining Protein Complex Structures Based on a Bayesian Model of in Vivo Förster Resonance Energy Transfer (FRET) Data

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