Skip to main content

ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating

Author(s): Rogers, Jason V; Arlow, Tim; Inkellis, Elizabeth R; Koo, Timothy S; Rose, Mark D

To refer to this page use:
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.
Publication Date: 15-Dec-2013
Citation: Rogers, Jason V, Arlow, Tim, Inkellis, Elizabeth R, Koo, Timothy S, Rose, Mark D. (2013). ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating. Molecular Biology of the Cell, 24 (24), 3896 - 3908. doi:10.1091/mbc.e13-08-0441
DOI: doi:10.1091/mbc.e13-08-0441
ISSN: 1059-1524
EISSN: 1939-4586
Pages: 3896 - 3908
Type of Material: Journal Article
Journal/Proceeding Title: Molecular Biology of the Cell
Version: Final published version. This is an open access article.

Items in OAR@Princeton are protected by copyright, with all rights reserved, unless otherwise indicated.