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ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating
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 loca...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3861085/ https://www.ncbi.nlm.nih.gov/pubmed/24152736 http://dx.doi.org/10.1091/mbc.E13-08-0441 |
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author | Rogers, Jason V. Arlow, Tim Inkellis, Elizabeth R. Koo, Timothy S. Rose, Mark D. |
author_facet | Rogers, Jason V. Arlow, Tim Inkellis, Elizabeth R. Koo, Timothy S. Rose, Mark D. |
author_sort | Rogers, Jason V. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3861085 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-38610852014-03-02 ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating Rogers, Jason V. Arlow, Tim Inkellis, Elizabeth R. Koo, Timothy S. Rose, Mark D. Mol Biol Cell Articles 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. The American Society for Cell Biology 2013-12-15 /pmc/articles/PMC3861085/ /pubmed/24152736 http://dx.doi.org/10.1091/mbc.E13-08-0441 Text en © 2013 Rogers et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Rogers, Jason V. Arlow, Tim Inkellis, Elizabeth R. Koo, Timothy S. Rose, Mark D. ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating |
title | ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating |
title_full | ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating |
title_fullStr | ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating |
title_full_unstemmed | ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating |
title_short | ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating |
title_sort | er-associated snares and sey1p mediate nuclear fusion at two distinct steps during yeast mating |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3861085/ https://www.ncbi.nlm.nih.gov/pubmed/24152736 http://dx.doi.org/10.1091/mbc.E13-08-0441 |
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