ArticleMicrobiologyOpen2014
Fpk1/2 kinases regulate cellular sphingoid long-chain base abundance and alter cellular resistance to LCB elevation or depletion.
Article in MicrobiologyOpen, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- The Ypk1 protein kinase signaling pathway is rewired and not essential for viability in Candida albicans.PLoS genetics · 2023Article
- Article
- A critical role of farnesol in the modulation of Amphotericin B and Aureobasidin A antifungal drug susceptibility.Mycology · 2022Article
- An optogenetic system to control membrane phospholipid asymmetry through flippase activation in budding yeast.Scientific reports · 2020Article
- Pho85 and PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2020Article
- TOR Complex 2-Regulated Protein Kinase Fpk1 Stimulates Endocytosis via Inhibition of Ark1/Prk1-Related Protein Kinase Akl1 in Saccharomyces cerevisiae.Molecular and cellular biology · 2017Article
- Control of Plasma Membrane Permeability by ABC Transporters.Eukaryotic cell · 2015Article
- Protein kinase Gin4 negatively regulates flippase function and controls plasma membrane asymmetry.The Journal of cell biology · 2015Article
- TORC1 promotes phosphorylation of ribosomal protein S6 via the AGC kinase Ypk3 in Saccharomyces cerevisiae.PloS one · 2015Article
- TOR complex 2-Ypk1 signaling regulates actin polarization via reactive oxygen species.Molecular biology of the cell · 2014Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sphingolipids are a family of eukaryotic lipids biosynthesized from sphingoid long-chain bases (LCBs). Sphingolipids are an essential class of lipids, as their depletion results in cell death. However, acute LCB supplementation is also toxic; thus, proper cellular LCB levels should be maintained. To characterize the "sphingolipid-signaling intercross," we performed a kinome screening assay in which budding yeast protein kinase-knockout strains were screened for resistance to ISP-1, a potent inhibitor of LCB biosynthesis. Here, one pair of such DIR (deletion-mediated ISP-1 resistance) genes, FPK1 and FPK2, was further characterized. Cellular LCB levels increased in the fpk1/2∆ strain, which was hypersensitive to phytosphingosine (PHS), a major LCB species of yeast cells. Concomitantly, this strain acquired resistance to ISP-1. Fpk1 and Fpk2 were involved in two downstream events; that is, ISP-1 uptake due to aminophospholipid flippase and LCB degradation due to LCB4 expression. RSK3, which belongs to the p90-S6K subfamily, was identified as a functional counterpart of Fpk1/2 in mammalian cells as the RSK3 gene functionally complemented the ISP-1-resistant phenotype of fpk1/2∆ cells.
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