FSH1encodes lysophospholipase activity inSaccharomyces cerevisiae

Objectives To elucidate the role ofFSH1(family of serine hydrolase) in lipid homeostasis. Results Proteins in various species containing alpha/beta hydrolase domain are known to be involved in lipid metabolism. In silico analysis of theFSH1gene inSaccharomyces cerevisiaerevealed the presence of alpha/beta hydrolase domain (ABHD) and a lipase motif (GXSXG), however its function in lipid metabolism remained elusive. The overexpression ofFSH1in WT andfsh1 Delta cells showed a significant reduction in the cellular phospholipid levels and an increase in the triacylglycerol levels and lipid droplet (LD) number. Furthermore, the purified recombinant protein Fsh1p was identified as a lysophospholipase that specifically acts on lysophosphatidylserine (LPS) and impacts the lipid homeostasis inS. cerevisiae. Conclusions These results depicted that Fsh1p has a role on lipid homeostasis and is a lysophospholipase that hydrolyzes lysophosphatidylserine (LPS).

Automated summary

The study revealed the role of FSH1 in lipid metabolism. Overexpression of FSH1 led to decreased cellular phospholipid levels, increased triacylglycerol levels, and influenced lipid droplet numbers. The purified recombinant protein Fsh1p was identified as a lysophospholipase that hydrolyzes lysophosphatidylserine (LPS) and impacts lipid homeostasis in S. cerevisiae.