LCB5/YLR260W Summary Help

LCB5 BASIC INFORMATION

Standard Name LCB5
Systematic Name YLR260W
Feature Type ORF, Verified
Description Minor sphingoid long-chain base kinase, paralog of Lcb4p responsible for few percent of the total activity, possibly involved in synthesis of long-chain base phosphates, which function as signaling molecules (1 and see Summary Paragraph)
Name Description Long-Chain Base 1
GO Annotations All LCB5 GO evidence and references
    View Computational GO annotations for LCB5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Pathways
Mutant Phenotype All LCB5 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions LCB5 All interactions details and references
9 total interaction(s) for 8 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • PCA: 1

Genetic Interactions
  • Phenotypic Enhancement: 3
  • Phenotypic Suppression: 1
  • Synthetic Growth Defect: 2

Sequence Information
ChrXII:665846 to 667909 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 2004-02-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2064 665846..667909 2004-02-05 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000004250

LCB5 RESOURCES

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SGD ORF map
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

SUMMARY PARAGRAPH for LCB5

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)(2). 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 (3). 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 heat stress response (4, 5). 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 (6). Since phosphoinositol-containing sphingolipids are unique to fungi, the sphingolipid biosynthesis pathway is considered a target for antifungal drugs (7, 8).

Last updated: 2007-10-05

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for LCB5]

1) Nagiec MM, et al.  (1998) The LCB4 (YOR171c) and LCB5 (YLR260w) genes of Saccharomyces encode sphingoid long chain base kinases. J Biol Chem 273(31):19437-42
2) Dickson RC and Lester RL  (2002) Sphingolipid functions in Saccharomyces cerevisiae. Biochim Biophys Acta 1583(1):13-25
3) 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
4) Jenkins GM, et al.  (1997) Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae. J Biol Chem 272(51):32566-72
5) 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
6) 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
7) 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
8) Sugimoto Y, et al.  (2004) IPC synthase as a useful target for antifungal drugs. Curr Drug Targets Infect Disord 4(4):311-22