LCB2/YDR062W Summary Help

Standard Name LCB2 1 (see Nomenclature conflict Note)
Systematic Name YDR062W
Alias SCS1 2 , TSC1
Feature Type ORF, Verified
Description Component of serine palmitoyltransferase, responsible along with Lcb1p for the first committed step in sphingolipid synthesis, which is the condensation of serine with palmitoyl-CoA to form 3-ketosphinganine (1, 2 and see Summary Paragraph)
Name Description Long-Chain Base 1, 3
Chromosomal Location
ChrIV:576474 to 578159 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All LCB2 GO evidence and references
  View Computational GO annotations for LCB2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Pathways
Mutant phenotypes All LCB2 Phenotype evidence and references
Classical genetics
null
repressible
Large-scale survey
conditional
null
reduction of function
Resources
interactions All LCB2 Interaction evidence and references
93 total interaction(s) for 59 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 36
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 7
  • PCA: 1
  • Reconstituted Complex: 1
Genetic Interactions
  • Negative Genetic: 27
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Positive Genetic: 7
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 4
  • Synthetic Rescue: 6
Resources
Expression Summary
histogram
Resources
Protein Information All LCB2 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:576474 to 578159 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1686 576474..578159 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002469

NOMENCLATURE CONFLICT NOTE

NameRelevanceDescription
RTS1Nomenclature conflictSCS1 has been used in the literature to refer to both RTS1/YOR014W, which encodes a protein phosphatase 2A and LCB2/YDR062W, which encodes a serine C-palmitoyltransferase.
INO2Nomenclature conflictSCS1 has been used to describe both INO2/YDR123C, a transcription factor involved in phospholipid synthesis, and LCB2/YDR062W, a serine C-palmitoyltransferase involved in sphingolipid biosynthesis.
SUMMARY PARAGRAPH for LCB2

About sphingolipid metabolism

Sphingolipids are essential components of the plasma membrane in all eukaryotic cells. S. cerevisiae cells make three complex sphingolipids: inositol-phosphoceramide (IPC), mannose-inositol-phosphoceramide (MIPC), and mannose-(inositol phosphate)2-ceramide (M(IP)2C)(4). In the yeast plasma membrane sphingolipids concentrate with ergosterol to form lipid rafts, specialized membrane microdomains implicated in a variety of cellular processes, including sorting of membrane proteins and lipids, as well as organizing and regulating signaling cascades (5). Intermediates in sphingolipid biosynthesis have been shown to play important roles as signaling molecules and growth regulators. Sphingolipid long chain bases (LCBs), dihydrosphingosine (DHS) and phytosphingosine (PHS), have been implicated as secondary messengers in signaling pathways that regulate the heat stress response (6, 7). Other intermediates, phytoceramide and long-chain base phosphates (LCBPs), have been shown to be components of the tightly-controlled ceramide/LCBP rheostat, which regulates cell growth (8). Since phosphoinositol-containing sphingolipids are unique to fungi, the sphingolipid biosynthesis pathway is considered a target for antifungal drugs (9, 10).

Last updated: 2007-10-05

References cited on this page View Complete Literature Guide for LCB2
1) Nagiec MM, et al.  (1994) The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis. Proc Natl Acad Sci U S A 91(17):7899-902
2) Zhao C, et al.  (1994) Suppressors of the Ca(2+)-sensitive yeast mutant (csg2) identify genes involved in sphingolipid biosynthesis. Cloning and characterization of SCS1, a gene required for serine palmitoyltransferase activity. J Biol Chem 269(34):21480-8
3) Pinto WJ, et al.  (1992) Sphingolipid long-chain-base auxotrophs of Saccharomyces cerevisiae: genetics, physiology, and a method for their selection. J Bacteriol 174(8):2565-74
4) Dickson RC and Lester RL  (2002) Sphingolipid functions in Saccharomyces cerevisiae. Biochim Biophys Acta 1583(1):13-25
5) Bagnat M and Simons K  (2002) Lipid rafts in protein sorting and cell polarity in budding yeast Saccharomyces cerevisiae. Biol Chem 383(10):1475-80
6) Jenkins GM, et al.  (1997) Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae. J Biol Chem 272(51):32566-72
7) Ferguson-Yankey SR, et al.  (2002) Mutant analysis reveals complex regulation of sphingolipid long chain base phosphates and long chain bases during heat stress in yeast. Yeast 19(7):573-86
8) Kobayashi SD and Nagiec MM  (2003) Ceramide/long-chain base phosphate rheostat in Saccharomyces cerevisiae: regulation of ceramide synthesis by Elo3p and Cka2p. Eukaryot Cell 2(2):284-94
9) Nagiec MM, et al.  (1997) Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J Biol Chem 272(15):9809-17
10) Sugimoto Y, et al.  (2004) IPC synthase as a useful target for antifungal drugs. Curr Drug Targets Infect Disord 4(4):311-22