SLM2 phosphatidylinositol 4,5-bisphosphate-binding protein [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: SLM2
Official Full Name: phosphatidylinositol 4,5-bisphosphate-binding protein
Primary source: SGD:S000004992
Locus tag: YNL047C
See related: AllianceGenome:SGD:S000004992; FungiDB:YNL047C; VEuPathDB:YNL047C
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: LIT1
Summary: Predicted to enable phosphatidylinositol 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, Dec 2024]
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Genomic context

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See SLM2 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (539911..541881, complement)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
TORC2 has been shown previously to negatively regulate calcineurin in part by phosphorylating two related proteins, Slm1 and Slm2, which associate with the PM via plextrin homology domains
Title: Plasma membrane recruitment and activation of the AGC kinase Ypk1 is mediated by target of rapamycin complex 2 (TORC2) and its effector proteins Slm1 and Slm2.
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.
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.
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.
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.

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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

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables phosphatidylinositol binding	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in TOR signaling	IPI Inferred from Physical Interaction more info	PubMed
involved_in actin cytoskeleton organization	IBA Inferred from Biological aspect of Ancestor more info
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 cell periphery	HDA more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
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_014351.3

Phosphoinositide PI4,5P(2) binding protein, forms a complex with Slm1p; acts downstream of Mss4p in a pathway regulating actin cytoskeleton organization in response to stress; TORC2 complex substrate and effector; SLM2 has a paralog, SLM1, 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

NC_001146.8 Reference assembly

Range

539911..541881 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182886.3 → NP_014351.3 TPA: phosphatidylinositol 4,5-bisphosphate-binding protein [Saccharomyces cerevisiae S288C]

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W1D2, P53955, Q2VQW4

UniProtKB/TrEMBL

G2WM56, N1P4J1

Conserved Domains (1) summary

cd13311
Location:444 → 555

PH_Slm1; Slm1 Pleckstrin homology (PH) domain