PIL1 lipid-binding protein PIL1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PIL1
Official Full Name: lipid-binding protein PIL1
Primary source: SGD:S000003318
Locus tag: YGR086C
See related: AllianceGenome:SGD:S000003318; FungiDB:YGR086C; VEuPathDB:YGR086C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables lipid binding activity. Involved in eisosome assembly; endocytosis; and protein localization to eisosome filament. Located in eisosome and mitochondrial outer membrane. [provided by Alliance of Genome Resources, Jul 2025]
Orthologs: all
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Genomic context

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See PIL1 in Genome Data Viewer

Location:: chromosome: VII

Exon count:: 1

Sequence:: Chromosome: VII; NC_001139.9 (649598..650617, complement)

Chromosome VII - NC_001139.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Lsp1 partially substitutes for Pil1 function in eisosome assembly under stress conditions.
Title: Lsp1 partially substitutes for Pil1 function in eisosome assembly under stress conditions.
Eisosome protein Pil1 regulates mitochondrial morphology, mitophagy, and cell death in Saccharomyces cerevisiae.
Title: Eisosome protein Pil1 regulates mitochondrial morphology, mitophagy, and cell death in Saccharomyces cerevisiae.
Plasma membrane tension regulates eisosome structure and function.
Title: Plasma membrane tension regulates eisosome structure and function.
Combined cryo-fluorescence microscopy with electron cryo-tomography results demonstrate that in cells, the BAR protein Pil1 localizes to eisosomes of varying membrane curvature. Further analysis revealed a dense protein coat on curved eisosomes, which was not present on shallow eisosomes, indicating that while BAR domains can assemble at shallow membranes, scaffold formation is tightly coupled to curvature generation.
Title: Correlative Microscopy of Vitreous Sections Provides Insights into BAR-Domain Organization In Situ.
In cells lacking the eisosome organizer Pil1, Xrn1 does not associate with the plasma membrane and its activity is preserved till the stationary phase. Thus, properly assembled eisosome is necessary for this kind of Xrn1 regulation, which occurs in a liquid culture as well as in a differentiated colony.
Title: mRNA decay is regulated via sequestration of the conserved 5'-3' exoribonuclease Xrn1 at eisosome in yeast.
Data indicate that Pkc1-induced phosphorylation of the eisosome core components Pil1 and Lsp1 was not exerted directly by Pkc1, but involved signaling through the Slt2 MAPK module.
Title: Phosphoproteomic analysis of protein kinase C signaling in Saccharomyces cerevisiae reveals Slt2 mitogen-activated protein kinase (MAPK)-dependent phosphorylation of eisosome core components.
Seg1/Sle1 controls eisosome assembly and shape, which also involves Pil1 and Lsp1
Title: Seg1 controls eisosome assembly and shape.
Pil1 and Lsp1 self-assemble into higher-order structures and bind preferentially to phosphoinositide-containing membranes.
Title: Eisosome proteins assemble into a membrane scaffold.
Pil1, an eisosome organizer, plays an important role in the recruitment of synaptojanins and amphiphysins to facilitate receptor-mediated endocytosis in yeast
Title: Pil1, an eisosome organizer, plays an important role in the recruitment of synaptojanins and amphiphysins to facilitate receptor-mediated endocytosis in yeast.
Pil1 expression is regulated by the cell cycle, which synchronizes eisosome formation with plasma membrane growth.
Title: Pil1 controls eisosome biogenesis.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables lipid binding	IBA Inferred from Biological aspect of Ancestor more info
enables lipid binding	IDA Inferred from Direct Assay more info	PubMed
enables lipid binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in eisosome assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in eisosome assembly	IEA Inferred from Electronic Annotation more info
involved_in eisosome assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in endocytosis	IBA Inferred from Biological aspect of Ancestor more info
involved_in endocytosis	IEA Inferred from Electronic Annotation more info
involved_in endocytosis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in intracellular protein localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein localization to eisosome filament	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cell periphery	HDA more info	PubMed
located_in cytoplasm	HDA more info	PubMed
located_in eisosome	IDA Inferred from Direct Assay more info	PubMed
located_in eisosome	IEA Inferred from Electronic Annotation more info
part_of eisosome filament	IBA Inferred from Biological aspect of Ancestor more info
located_in lipid droplet	IEA Inferred from Electronic Annotation more info
located_in mitochondrial outer membrane	HDA more info	PubMed
located_in mitochondrial outer membrane	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed
located_in plasma membrane	HDA more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: lipid-binding protein PIL1

NP_011600.3

Eisosome core component involved in endocytosis; mitochondria phosphoprotein that localizes to the outer membrane and is involved in maintaining mitochondrial morphology and mitophagy; phosphorylated (T233) upon Pkc1p hyperactivation in a Slt2p MAPK-dependent fashion; null mutant shows activation of Pkc1p/Ypk1p stress resistance pathways; BAR domain family member; protein increases in abundance and relocalizes from the plasma membrane to cytoplasm upon DNA replication stress