Binding interactions control SNARE specificity in vivo

Yang, Hui-Ju; Nakanishi, Hideki; Liu, Song; McNew, James A.; Neiman, Aaron M.

doi:10.1083/jcb.200809178

Cited by 16 publications

(19 citation statements)

References 45 publications

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“…Sso1/2 and Sec9 form a binary complex on the plasma membrane that interacts with Snc1/2 arriving with the vesicle to create the active fusogen (Rossi et al 1997;McNew et al 2000). At the prospore membrane, vesicle fusion requires Sso1, Snc1/2, and a sporulation-specific Sec9 paralog called Spo20, whereas Sec9 and Sso2 are not required (Neiman 1998;Jantti et al 2002;Yang et al 2008). It is the presence of Sec9 vs. Spo20 that determines at which membranes the complex will function (Neiman et al 2000); even when their expression patterns are reversed, neither protein can substitute for the other (Neiman 1998).…”

Section: Key Events In the Phases Of Sporulationmentioning

confidence: 99%

“…Prospore membrane initiation: Docking of vesicles onto the MOP is a necessary prerequisite for prospore membrane formation, but the fusion of vesicles also requires additional factors such as a SNARE complex that acts specifically at the prospore membrane (Neiman 1998;Jantti et al 2002;Yang et al 2008). SNAREs act as fusogens in intracellular membrane transport events and different combinations of SNAREs mediate fusion at different organelles (Pelham 1999(Pelham , 2001).…”

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: 99%

Section: Key Events In the Phases Of Sporulationmentioning

confidence: 99%

Sporulation in the Budding Yeast Saccharomyces cerevisiae

2011

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“…The membrane cap is expanded to form a membrane sac by additional vesicle fusion before completion of the formation of the prospore membrane. This vesicle fusion requires a SNARE complex that is formed by Sso1p, Snc1/2p, and Spo20p (1196,1197) and other upstream proteins required for vegetative growth. Spo20p, a sporulation-specific protein, directs the complex to function on the prospore membrane rather than plasma membrane (1198).…”

Section: Sexual Developmentmentioning

confidence: 99%

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Schmoll

Dattenböck

Carreras-Villaseñor

et al. 2016

Microbiol Mol Biol Rev

163

195

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SUMMARYThe genusTrichodermacontains fungi with high relevance for humans, with applications in enzyme production for plant cell wall degradation and use in biocontrol. Here, we provide a broad, comprehensive overview of the genomic content of these species for “hot topic” research aspects, including CAZymes, transport, transcription factors, and development, along with a detailed analysis and annotation of less-studied topics, such as signal transduction, genome integrity, chromatin, photobiology, or lipid, sulfur, and nitrogen metabolism inT. reesei,T. atroviride, andT. virens, and we open up new perspectives to those topics discussed previously. In total, we covered more than 2,000 of the predicted 9,000 to 11,000 genes of eachTrichodermaspecies discussed, which is >20% of the respective gene content. Additionally, we considered available transcriptome data for the annotated genes. Highlights of our analyses include overall carbohydrate cleavage preferences due to the different genomic contents and regulation of the respective genes. We found light regulation of many sulfur metabolic genes. Additionally, a new Golgi 1,2-mannosidase likely involved inN-linked glycosylation was detected, as were indications for the ability ofTrichodermaspp. to generate hybrid galactose-containingN-linked glycans. The genomic inventory of effector proteins revealed numerous compounds unique toTrichoderma, and these warrant further investigation. We found interesting expansions in theTrichodermagenus in several signaling pathways, such as G-protein-coupled receptors, RAS GTPases, and casein kinases. A particularly interesting feature absolutely unique toT. atrovirideis the duplication of the alternative sulfur amino acid synthesis pathway.

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“…The Ssop/Sec9p binary complex forms a more efficient SNAREpin than the Ssop/Spo20p complex, with the Sso2p/Spo20p complex the least fusogenic of the four possible t-SNARE complexes (30). Mutation of a glutamine within the ionic layer of the H3 motif of Sso1p impaired its ability to interact with Spo20p and resulted in a decrease in sporulation efficiency, suggesting that small changes in related SNARE helices can affect interactions between cognate SNAREs and hence effect intracellular fusion specificity (59). However, the glutamine residue within the H3 of Sso1p is also present in Sso2p, suggesting that this interaction alone cannot explain the specificity of Sso1p for PSM formation.…”

Section: Discussionmentioning

confidence: 99%

Phosphatidylinositol-4,5-Bisphosphate and Phospholipase D-Generated Phosphatidic Acid Specify SNARE-Mediated Vesicle Fusion for Prospore Membrane Formation

Mendonsa

Engebrecht

2009

Eukaryot Cell

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The soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) family of proteins is required for eukaryotic intracellular membrane fusions. Vesicle fusion for formation of the prospore membrane (PSM), a membrane compartment that forms de novo during yeast sporulation, requires SNARE function, phosphatidylinositol-4,5-bisphosphate [PI(4,5)P 2 ], and the activity of the phospholipase D (PLD) Spo14p, which generates phosphatidic acid (PA). The SNARE syntaxin Sso1p is essential for PSM production while the functionally redundant homolog in vegetative growth, Sso2p, is not. We demonstrate that Sso1p and Sso2p bind similarly in vitro to PA or phosphoinositide-containing liposomes and that the conserved SNARE (H3) domain largely mediates PA-binding. Both green fluorescent protein-Sso fusion proteins localize to the developing PSM in wild-type cells and to the spindle pole body in spo14⌬ cells induced to sporulate. However, the autoregulatory region of Sso1p binds PI(4,5)P 2 -containing liposomes in vitro with a greater ability than the equivalent region of Sso2p. Overexpression of the phosphatidylinositol-4-phosphate 5-kinase MSS4 in sso1⌬ cells induced to sporulate stimulates PSM production; PLD activity is not increased under these conditions, indicating that PI(4,5)P 2 has roles in addition to stimulating PLD in PSM formation. These data suggest that PLD-generated PA and PI(4,5)P 2 collaborate at multiple levels to promote SNARE-mediated fusion for PSM formation.The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family of proteins is required for the fusion of vesicles to target membranes in eukaryotic cells (53). The process of SNARE-mediated fusion is both structurally and mechanistically similar in different intracellular transport pathways and is evolutionarily conserved from yeast to human (18,31,34). In vitro experiments demonstrated that SNAREs have the ability to effect fusions of liposomes in the absence of other components, indicating that these proteins directly mediate the fusion event (56). SNAREs can be broadly categorized as either vesicle SNAREs (v-SNAREs) or target membrane SNAREs (t-SNAREs), respectively. The interaction of SNAREs on apposed membranes can overcome the energy barrier generated by charged headgroups of lipids comprising the bilayers. As an incoming vesicle approaches its target membrane, the v-SNAREs and t-SNAREs assemble via their SNARE domains into a four-helix bundle termed a SNAREpin, bringing the two bilayers into closer proximity (3, 55, 56). The outer membrane layers of both the vesicle and target membrane mix, forming a hemifusion intermediate before full fusion of the membranes occurs (23,24,29,58).The helices comprising the SNAREpin are supplied by three different SNARE subfamilies. Two of these subfamily members, syntaxin and SNAP-25, are t-SNAREs; the former contributes one helix while the latter contributes two helices (16).The syntaxin and SNAP-25 homologs heterodimerize to form the t-SNARE complex before the trans-inte...

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Binding interactions control SNARE specificity in vivo

Cited by 16 publications

References 45 publications

Sporulation in the Budding Yeast Saccharomyces cerevisiae

Sporulation in the Budding Yeast Saccharomyces cerevisiae

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Phosphatidylinositol-4,5-Bisphosphate and Phospholipase D-Generated Phosphatidic Acid Specify SNARE-Mediated Vesicle Fusion for Prospore Membrane Formation

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