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Lsp1 partially substitutes for Pil1 function in eisosome assembly under stress conditions.
Petra Vesela1, Jakub Zahumensky1, Jan Malinsky1
1Department of Functional Organization of Biomembranes, Institute of Experimental Medicine, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic.
Journal of Cell Science
|January 5, 2023
Summary
Lsp1 protein can organize fungal eisosomes under stress conditions when Pil1 is absent. This eisosome assembly involves Seg1 and Nce102, impacting cellular processes like oxidative phosphorylation.
Area of Science:
- Cell biology
- Mycology
- Biochemistry
Background:
- Eisosomes are vital plasma membrane structures in fungi, organized by Pil1 family BAR-domain proteins.
- Pil1 and Lsp1 are key proteins in Saccharomyces cerevisiae eisosome formation.
- Loss of PIL1 typically prevents eisosome assembly.
Purpose of the Study:
- To investigate eisosome assembly under stress conditions in the absence of Pil1.
- To identify alternative proteins involved in eisosome formation.
- To explore the functional connections of eisosomes with cellular processes.
Main Methods:
- Genetic manipulation of yeast strains (pil1Δ, seg1Δnce102Δpil1Δ).
- Analysis of eisosome assembly under hyperosmotic stress.
- Next-generation sequencing (RNA-seq) to assess gene expression changes.
Main Results:
- Lsp1 partially rescues eisosome formation in pil1Δ cells under specific stress conditions (e.g., reduced serine palmitoyltransferase activity).
- Seg1 and Nce102 are required for Lsp1-mediated eisosome assembly in the absence of Pil1.
- The seg1Δnce102Δpil1Δ strain shows altered gene expression, with upregulation of oxidative phosphorylation/TCA cycle genes and downregulation of DNA repair/ribosome biogenesis/cell cycle genes.
Conclusions:
- Lsp1 acts as a stress-responsive eisosome organizer, substituting for Pil1.
- Eisosome assembly is linked to cellular metabolism and stress response pathways.
- Novel functional connections exist between eisosomes and essential cellular processes like gene expression regulation and cell cycle control.
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