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SLM1 phosphatidylinositol 4,5-bisphosphate-binding protein [ Saccharomyces cerevisiae S288C ]

Gene ID: 854701, updated on 2-Nov-2024

Summary

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Official Symbol
SLM1
Official Full Name
phosphatidylinositol 4,5-bisphosphate-binding protein
Primary source
SGD:S000001367
Locus tag
YIL105C
See related
AllianceGenome:SGD:S000001367; FungiDB:YIL105C; VEuPathDB:YIL105C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
LIT2
Summary
Enables phosphatidylinositol-4,5-bisphosphate binding activity and sphingolipid binding activity. Involved in several processes, including TOR signaling; actin cytoskeleton organization; and eisosome assembly. Located in plasma membrane. [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See SLM1 in Genome Data Viewer
Location:
chromosome: IX
Exon count:
1
Sequence:
Chromosome: IX; NC_001141.2 (167581..169641, complement)

Chromosome IX - NC_001141.2Genomic Context describing neighboring genes Neighboring gene 6-phosphofructo-2-kinase Neighboring gene Mob1p Neighboring gene uncharacterized protein Neighboring gene Hsp90 cochaperone SHQ1 Neighboring gene 2-(3-amino-3-carboxypropyl)histidine synthase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001141.2

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structural analyses of the Slm1-PH domain demonstrate ligand binding in the non-canonical site. Anand K, et al. PLoS One, 2012. PMID 22574179, Free PMC Article
  2. Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae. Niles BJ, et al. Cell Cycle, 2012 Oct 15. PMID 22895050, Free PMC Article
  3. Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae. Kamble C, et al. J Biosci, 2011 Mar. PMID 21451250
  4. Plasma membrane tension regulates eisosome structure and function. Appadurai D, et al. Mol Biol Cell, 2020 Feb 15. PMID 31851579, Free PMC Article
  5. The eisosome core is composed of BAR domain proteins. Olivera-Couto A, et al. Mol Biol Cell, 2011 Jul 1. PMID 21593205, Free PMC Article

See all (88) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Plasma membrane tension regulates eisosome structure and function.
    Title: Plasma membrane tension regulates eisosome structure and function.
  2. Slm1/Slm2 and TORC2-dependent phosphorylation of Ypk1 is coupled to the biosynthesis of complex sphingolipids and to their levels within the plasma membrane.
    Title: Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae.
  3. Slm proteins are required for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae.
    Title: Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae.
  4. Slm proteins are subject to regulation by multiple signals, including PI4,5P(2), TORC2, and sphingolipids, and may thus integrate inputs from different signaling pathways to temporally and spatially control actin polarization
    Title: The yeast PH domain proteins Slm1 and Slm2 are targets of sphingolipid signaling during the response to heat stress.
  5. Slm1 and Slm2 integrate inputs from the Phosphatidylinositol-4,5-bisphosphate and TORC2 to modulate polarized actin assembly and growth
    Title: The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2.
  6. Data suggest that Slm1 and Slm2 define a molecular link between phosphoinositide and sphingolipid signaling and thereby regulate actin cytoskeleton organization.
    Title: The phosphatidylinositol 4,5-biphosphate and TORC2 binding proteins Slm1 and Slm2 function in sphingolipid regulation.
  7. calcineurin may modulate sphingolipid-dependent events through regulation of Slm1 and Slm2
    Title: Slm1 and slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables phosphatidylinositol-4,5-bisphosphate binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables sphingolipid binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in TOR signaling IPI
Inferred from Physical Interaction
more info
 PubMed 
involved_in actin cytoskeleton organization IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in actin filament bundle assembly IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in eisosome assembly IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in endosomal transport IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in establishment or maintenance of actin cytoskeleton polarity IPI
Inferred from Physical Interaction
more info
 PubMed 
involved_in protein localization to plasma membrane IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in regulation of cell growth IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in regulation of cell growth IPI
Inferred from Physical Interaction
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm HDA PubMed 
located_in mitochondrion HDA PubMed 
located_in plasma membrane HDA PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
phosphatidylinositol 4,5-bisphosphate-binding protein
NP_012161.1
  • Phosphoinositide PI4,5P(2) binding protein, forms a complex with Slm2p; acts downstream of Mss4p in a pathway regulating actin cytoskeleton organization in response to stress; TORC2 complex substrate and effector; protein abundance increases in response to DNA replication stress; SLM1 has a paralog, SLM2, that arose from the whole genome duplication

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001141.2 Reference assembly

    Range
    167581..169641 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001179453.1 → NP_012161.1  TPA: phosphatidylinositol 4,5-bisphosphate-binding protein [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_012161.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VVI2, P40485
    UniProtKB/TrEMBL
    B3LTV2, B5VKK5, C7GKN1
    Conserved Domains (1) summary
    cd13311
    Location:467 → 581
    PH_Slm1; Slm1 Pleckstrin homology (PH) domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P40485.1

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