ArticleMolecular biology of the cell2013
ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Plasmodium SEY1 is a novel druggable target that contributes to imidazolopiperazine mechanism of action.Research square · 2024Article
- Protein S-palmitoylation regulates different stages of meiosis inLife science alliance · 2023Article
- Evolution of factors shaping the endoplasmic reticulum.Traffic (Copenhagen, Denmark) · 2022Article
- The Dynamin-Like GTPase FgSey1 Plays a Critical Role in Fungal Development and Virulence in Fusarium graminearum.Applied and environmental microbiology · 2020Article
- Assembly-hub function of ER-localized SNARE proteins in biogenesis of tombusvirus replication compartment.PLoS pathogens · 2018Article
- Digging deep into Golgi phenotypic diversity with unsupervised machine learning.Molecular biology of the cell · 2017Article
- The Malleable Nature of the Budding Yeast Nuclear Envelope: Flares, Fusion, and Fenestrations.Journal of cellular physiology · 2016Review
- Arabidopsis Qc-SNARE genes BET11 and BET12 are required for fertility and pollen tube elongation.Botanical studies · 2015Article
- SNAREs support atlastin-mediated homotypic ER fusion in Saccharomyces cerevisiae.The Journal of cell biology · 2015Article
- Cell biology of yeast zygotes, from genesis to budding.Biochimica et biophysica acta · 2015Review
- Membrane Contact Sites: Complex Zones for Membrane Association and Lipid Exchange.Lipid insights · 2015Review
- Kar5p is required for multiple functions in both inner and outer nuclear envelope fusion in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2014Article
- ER-associated retrograde SNAREs and the Dsl1 complex mediate an alternative, Sey1p-independent homotypic ER fusion pathway.Molecular biology of the cell · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
During yeast mating, two haploid nuclei fuse membranes to form a single diploid nucleus. However, the known proteins required for nuclear fusion are unlikely to function as direct fusogens (i.e., they are unlikely to directly catalyze lipid bilayer fusion) based on their predicted structure and localization. Therefore we screened known fusogens from vesicle trafficking (soluble N-ethylmaleimide-sensitive factor attachment protein receptors [SNAREs]) and homotypic endoplasmic reticulum (ER) fusion (Sey1p) for additional roles in nuclear fusion. Here we demonstrate that the ER-localized SNAREs Sec20p, Ufe1p, Use1p, and Bos1p are required for efficient nuclear fusion. In contrast, Sey1p is required indirectly for nuclear fusion; sey1Δ zygotes accumulate ER at the zone of cell fusion, causing a block in nuclear congression. However, double mutants of Sey1p and Sec20p, Ufe1p, or Use1p, but not Bos1p, display extreme ER morphology defects, worse than either single mutant, suggesting that retrograde SNAREs fuse ER in the absence of Sey1p. Together these data demonstrate that SNAREs mediate nuclear fusion, ER fusion after cell fusion is necessary to complete nuclear congression, and there exists a SNARE-mediated, Sey1p-independent ER fusion pathway.
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