Structure of sterol aliphatic chains affects yeast cell shape and cell fusion during mating

Under mating conditions, yeast cells adopt a characteristic pear-shaped morphology, called a "shmoo," as they project a cell extension toward their mating partners. Mating partners make contact at their shmoo tips, dissolve the intervening cell wall, and fuse their plasma membranes. We ide...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2010-03, Vol.107 (9), p.4170-4175
Main Authors: Aguilar, Pablo S, Heiman, Maxwell G, Walther, Tobias C, Engel, Alex, Schwudke, Dominik, Gushwa, Nathan, Kurzchalia, Teymuras, Walter, Peter
Format: Article
Language:English
Subjects:
Biocatalysis
Biological Sciences
biosynthesis
cell biology
Cell Fusion
Cell growth
Cell membranes
Cell Shape
Cell size
Cell walls
Cells
Cytochrome P-450 Enzyme System - genetics
Cytology
Enzyme kinetics
Enzymes
ERG4 gene
Ergosterol
Ergosterol - biosynthesis
Gene Deletion
Genes, Fungal
Lipids
lipogenesis
Mating
Membranes
Morphology
Mutation
Oxidoreductases - genetics
Pheromones
Plant reproduction
plasma membrane
Plasma membranes
Reproductive efficiency
Saccharomyces cerevisiae
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins - genetics
sexual reproduction
shmoo cells
Sterols
Supplementation
Yeast
Yeasts
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Summary:Under mating conditions, yeast cells adopt a characteristic pear-shaped morphology, called a "shmoo," as they project a cell extension toward their mating partners. Mating partners make contact at their shmoo tips, dissolve the intervening cell wall, and fuse their plasma membranes. We identified mutations in ERG4, encoding the enzyme that catalyzes the last step of ergosterol biosynthesis, that impair both shmoo formation and cell fusion. Upon pheromone treatment, erg4Δ mutants polarized growth, lipids, and proteins involved in mating but did not form properly shaped shmoos and fused with low efficiency. Supplementation with ergosterol partially suppressed the shmooing defect but not the cell fusion defect. By contrast, removal of the Erg4 substrate ergosta-5,7,22,24(28)-tetraenol, which accumulates in erg4Δ mutant cells and contains an extra double bond in the aliphatic chain of the sterol, restored both shmooing and cell fusion to wild-type levels. Thus, a two-atom change in the aliphatic moiety of ergosterol is sufficient to obstruct cell shape remodeling and cell fusion.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0914094107