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Lucena Hernandez, R.

Publications and source records attributed to Lucena Hernandez, R..

2 recordsLinked to original sources

Lac1-dependent ceramide synthesis couples septum assembly to cell separation in Schizosaccharomyces pombe

Ceramides are precursors of complex sphingolipids and bioactive membrane lipids. In the fission yeast Schizosaccharomyces pombe, they are produced by a ceramide synthase with two catalytic subunits, Lac1 and Lag1, which are redundant but not functionally equivalent: only Lac1 is required for normal growth and cell size. Why Lac1 has this unique role, and how ceramide synthesis contributes to cell morphogenesis, remain unknown. Here, we show that Lac1 couples septum assembly to cell separation. Cells lacking Lac1 die predominantly during cell separation and build septa with a thinner primary layer and markedly thicker secondary layers, accompanied by altered deposition of {beta}-(1,3)-glucans and galactomannan. These defects are not rescued by osmotic stabilization. The essential glucan synthase Bgs4 is mislocalized to cytoplasmic granules, and total {beta}-(1,3)-glucan synthase activity is partially reduced. Nevertheless, Ags1, Bgs1 and Bgs4 accumulate to higher levels and persist almost twice as long at the division site, indicating defective clearance rather than delivery of the septum-synthesis machinery. Plasma membrane sterol distribution remains unaffected. To accurately impair ceramide synthesis, we isolated thermosensitive lac1-ts alleles in a lag1{Delta} background. Their substitutions cluster in the conserved TRAM/LAG1 domain. Metabolic labeling showed that these alleles reduce ceramide synthesis at the restrictive temperature. Molecular dynamics simulations indicated that two substitutions perturb distinct contacts with C26-CoA, while Lac1-M167T loses its endoplasmic reticulum localization. Acute inactivation recapitulates the deletion phenotype, causing septum accumulation and cell death. Together, our findings establish that Lac1-dependent ceramide synthesis is required for the orderly completion of septum assembly and cell separation.

cell biology↗

Uncoupling of nutrient sensing and cell size control by specific defects in ceramide structure

Ceramides are essential structural lipids whose chemical diversity arises from variations in acyl-chain length and sphingoid base modifications, yet how these structural features couple metabolic state to growth regulation remains unclear. In Saccharomyces cerevisiae, the TORC2-Ypk1/2 signaling axis coordinates plasma membrane homeostasis with cellular growth; however, the precise lipid-derived signals that modulate this pathway remain incompletely characterized. Here, we establish that the structural integrity of very-long-chain fatty acid (VLCFA)-containing ceramides is a critical determinant of nutrient-dependent cell size modulation and TORC2 activity. Disruption of VLCFA elongation elevates Ypk1/2 pT662, consistent with increased TORC2 output, in both nutrient conditions. We further discovered that yeast mutants in VLCFA elongation (elo3{Delta}), fail to modulate their cell size in response to nutrient deprivation. To separate VLCFA elongation from ceramide production, we expressed mammalian ceramide synthases with defined acyl-chain preferences. Ceramides with C24-C26 chains (CerS3) supported near-normal nutrient-dependent size modulation, whereas production of C22-C24 ceramides (CerS2) phenocopied elongation mutants, leading to hyperactive TORC2 signaling and defective size regulation. Remarkably, cells producing C18 ceramides retained size control despite elevated TORC2 activity, revealing that basal signaling and size regulation can be uncoupled. Furthermore, we identify a distinct role for hydroxylation. While sur2{Delta} mutants exhibited size regulation defects resembling elongation mutants, they retained normal nutrient-responsive TORC2 signaling. Conversely, scs7{Delta} mutants maintained normal size regulation but displayed reduced basal TORC2 activity. This striking uncoupling suggests that while the TORC2 pathway senses acyl chain length, sphingoid base hydroxylation is biophysically required downstream for the execution of cell size remodeling. Our findings demonstrate that distinct structural features of ceramides differentially regulate nutrient sensing, signaling intensity, and the mechanical execution of cell size control.

cell biology↗