ArticleCell cycle (Georgetown, Tex.)2017
A link between very long chain fatty acid elongation and mating-specific yeast cell cycle arrest.
Article in Cell cycle (Georgetown, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 8 citations in OpenAlex.
- Temporal oscillation of phospholipids promotes metabolic efficiency.Nature chemical biology · 2025Article
- Regulation of sphingolipid synthesis by the G1/S transcription factor Swi4.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021Article
- Discovery of broad-spectrum fungicides that block septin-dependent infection processes of pathogenic fungi.Nature microbiology · 2020Article
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5 authors at 2 institutions in 1 country.
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Abstract
Ceramides and sphingolipid intermediates are well-established regulators of the cell cycle. In the budding yeast Saccharomyces cerevisae, the complex sphingolipid backbone, ceramide, comprises a long chain sphingoid base, a polar head group, and a very long chain fatty acid (VLCFA). While ceramides and long chain bases have been extensively studied as to their roles in regulating cell cycle arrest under multiple conditions, the roles of VLCFAs are not well understood. Here, we used the yeast elo2 and elo3 mutants, which are unable to elongate fatty acids, as tools to explore if maintaining VLCFA elongation is necessary for cell cycle arrest in response to yeast mating. We found that both elo2 and elo3 cells had severely reduced mating efficiencies and were unable to form polarized shmoo projections that are necessary for cell-cell contact during mating. They also lacked functional MAP kinase signaling activity and were defective in initiating a cell cycle arrest in response to pheromone. Additional data suggests that mislocalization of the Ste5 scaffold in elo2 and elo3 mutants upon mating initiation may be responsible for the inability to initiate a cell cycle arrest. Moreover, the lack of proper Ste5 localization may be caused by the inability of mutant cells to mobilize PIP
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