DPL1/YDR294C Summary Help

Standard Name DPL1 (see Nomenclature conflict Note)
Systematic Name YDR294C
Alias BST1 1
Feature Type ORF, Verified
Description Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate (2, 3, 4 and see Summary Paragraph)
Name Description Dihydrosphingosine Phosphate Lyase
Chromosomal Location
ChrIV:1052228 to 1050459 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All DPL1 GO evidence and references
  View Computational GO annotations for DPL1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Pathways
Mutant phenotypes All DPL1 Phenotype evidence and references
Classical genetics
null
overexpression
Large-scale survey
null
overexpression
Resources
interactions All DPL1 Interaction evidence and references
70 total interaction(s) for 42 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Affinity Capture-Western: 1
  • Co-crystal Structure: 1
Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Rescue: 2
  • Negative Genetic: 36
  • Phenotypic Enhancement: 3
  • Phenotypic Suppression: 2
  • Positive Genetic: 7
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 5
  • Synthetic Rescue: 6
Resources
Expression Summary
histogram
Resources
Protein Information All DPL1 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:1052228 to 1050459 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
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..1770 1052228..1050459 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 SGDIDS000002702

NOMENCLATURE CONFLICT NOTE

NameRelevanceDescription
BST1Nomenclature conflictBoth YDR294C/DPL1 and YFL025C/BST1 have been referred to as BST1.
SUMMARY PARAGRAPH for DPL1

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)(5). 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 (6). 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 (7, 8). 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 (9). Since phosphoinositol-containing sphingolipids are unique to fungi, the sphingolipid biosynthesis pathway is considered a target for antifungal drugs (10, 11).

Last updated: 2007-10-05

References cited on this page View Complete Literature Guide for DPL1
1) Saba JD, et al.  (1997) The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-phosphate lyase. J Biol Chem 272(42):26087-90
2) Kim S, et al.  (2000) Accumulation of phosphorylated sphingoid long chain bases results in cell growth inhibition in Saccharomyces cerevisiae. Genetics 156(4):1519-29
3) Grote E, et al.  (2000) A snc1 endocytosis mutant: phenotypic analysis and suppression by overproduction of dihydrosphingosine phosphate lyase. Mol Biol Cell 11(12):4051-65
4) Zhang X, et al.  (2001) Elevation of endogenous sphingolipid long-chain base phosphates kills Saccharomyces cerevisiae cells. Curr Genet 40(4):221-33
5) Dickson RC and Lester RL  (2002) Sphingolipid functions in Saccharomyces cerevisiae. Biochim Biophys Acta 1583(1):13-25
6) 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
7) Jenkins GM, et al.  (1997) Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae. J Biol Chem 272(51):32566-72
8) 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
9) 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
10) 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
11) Sugimoto Y, et al.  (2004) IPC synthase as a useful target for antifungal drugs. Curr Drug Targets Infect Disord 4(4):311-22