The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

LCB1  -  serine C-palmitoyltransferase LCB1

Saccharomyces cerevisiae S288c

Synonyms: END8, Long chain base biosynthesis protein 1, SPT 1, SPT1, Serine palmitoyltransferase 1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of LCB1


High impact information on LCB1

  • Ceramide accumulation induced by S1P was completely blocked by fumonisin B1, an inhibitor of ceramide synthase, but only partially reduced by myriocin, an inhibitor of serine palmitoyltransferase, the first committed step in de novo synthesis of ceramide [6].
  • The Saccharomyces cerevisiae end8-1 mutant is allelic to lcb1, a mutant defective in the first step of sphingoid base synthesis [7].
  • Furthermore, partial RNA interference (RNAi) suppression of At LCB1 expression was accompanied by a marked reduction in plant size that resulted primarily from reduced cell expansion [8].
  • In yeast and mammalian cells, SPT is a heterodimer that consists of LCB1 and LCB2 subunits, which together form the active site of this enzyme [8].
  • These results demonstrate that plant SPT is a heteromeric enzyme and that sphingolipids are essential components of plant cells and contribute to growth and development [8].

Chemical compound and disease context of LCB1


Biological context of LCB1


Anatomical context of LCB1


Associations of LCB1 with chemical compounds


Physical interactions of LCB1

  • To determine whether Pas1 links nutrient availability to cell cycle progression downstream of the Tsc1/Tsc2 complex, we examined the kinetics of G1 arrest in single and double mutant strains [3].

Other interactions of LCB1


Analytical, diagnostic and therapeutic context of LCB1


  1. Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. Gable, K., Han, G., Monaghan, E., Bacikova, D., Natarajan, M., Williams, R., Dunn, T.M. J. Biol. Chem. (2002) [Pubmed]
  2. Cloning and characterization of LCB1, a Saccharomyces gene required for biosynthesis of the long-chain base component of sphingolipids. Buede, R., Rinker-Schaffer, C., Pinto, W.J., Lester, R.L., Dickson, R.C. J. Bacteriol. (1991) [Pubmed]
  3. Pas1, a G1 cyclin, regulates amino acid uptake and rescues a delay in G1 arrest in Tsc1 and Tsc2 mutants in Schizosaccharomyces pombe. van Slegtenhorst, M., Mustafa, A., Henske, E.P. Hum. Mol. Genet. (2005) [Pubmed]
  4. Role for de novo sphingoid base biosynthesis in the heat-induced transient cell cycle arrest of Saccharomyces cerevisiae. Jenkins, G.M., Hannun, Y.A. J. Biol. Chem. (2001) [Pubmed]
  5. Mutant SPTLC1 dominantly inhibits serine palmitoyltransferase activity in vivo and confers an age-dependent neuropathy. McCampbell, A., Truong, D., Broom, D.C., Allchorne, A., Gable, K., Cutler, R.G., Mattson, M.P., Woolf, C.J., Frosch, M.P., Harmon, J.M., Dunn, T.M., Brown, R.H. Hum. Mol. Genet. (2005) [Pubmed]
  6. Sphingosine-1-phosphate phosphohydrolase in regulation of sphingolipid metabolism and apoptosis. Le Stunff, H., Galve-Roperh, I., Peterson, C., Milstien, S., Spiegel, S. J. Cell Biol. (2002) [Pubmed]
  7. Sphingoid base synthesis requirement for endocytosis in Saccharomyces cerevisiae. Zanolari, B., Friant, S., Funato, K., Sütterlin, C., Stevenson, B.J., Riezman, H. EMBO J. (2000) [Pubmed]
  8. The Essential Nature of Sphingolipids in Plants as Revealed by the Functional Identification and Characterization of the Arabidopsis LCB1 Subunit of Serine Palmitoyltransferase. Chen, M., Han, G., Dietrich, C.R., Dunn, T.M., Cahoon, E.B. Plant Cell (2006) [Pubmed]
  9. Sphingolipids signal heat stress-induced ubiquitin-dependent proteolysis. Chung, N., Jenkins, G., Hannun, Y.A., Heitman, J., Obeid, L.M. J. Biol. Chem. (2000) [Pubmed]
  10. A mammalian homolog of the yeast LCB1 encodes a component of serine palmitoyltransferase, the enzyme catalyzing the first step in sphingolipid synthesis. Hanada, K., Hara, T., Nishijima, M., Kuge, O., Dickson, R.C., Nagiec, M.M. J. Biol. Chem. (1997) [Pubmed]
  11. Characterization of enzymatic synthesis of sphingolipid long-chain bases in Saccharomyces cerevisiae: mutant strains exhibiting long-chain-base auxotrophy are deficient in serine palmitoyltransferase activity. Pinto, W.J., Wells, G.W., Lester, R.L. J. Bacteriol. (1992) [Pubmed]
  12. Mutations in the Lcb2p subunit of serine palmitoyltransferase eliminate the requirement for the TSC3 gene in Saccharomyces cerevisiae. Monaghan, E., Gable, K., Dunn, T. Yeast (2002) [Pubmed]
  13. The topology of the Lcb1p subunit of yeast serine palmitoyltransferase. Han, G., Gable, K., Yan, L., Natarajan, M., Krishnamurthy, J., Gupta, S.D., Borovitskaya, A., Harmon, J.M., Dunn, T.M. J. Biol. Chem. (2004) [Pubmed]
  14. The identification of myriocin-binding proteins. Chen, J.K., Lane, W.S., Schreiber, S.L. Chem. Biol. (1999) [Pubmed]
  15. Fungal metabolite sulfamisterin suppresses sphingolipid synthesis through inhibition of serine palmitoyltransferase. Yamaji-Hasegawa, A., Takahashi, A., Tetsuka, Y., Senoh, Y., Kobayashi, T. Biochemistry (2005) [Pubmed]
  16. Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity. Gable, K., Slife, H., Bacikova, D., Monaghan, E., Dunn, T.M. J. Biol. Chem. (2000) [Pubmed]
  17. 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. Zhao, C., Beeler, T., Dunn, T. J. Biol. Chem. (1994) [Pubmed]
  18. Integrative transformation system for the metabolic engineering of the sphingoid base-producing yeast Pichia ciferrii. Bae, J.H., Sohn, J.H., Park, C.S., Rhee, J.S., Choi, E.S. Appl. Environ. Microbiol. (2003) [Pubmed]
  19. Expression of a Novel Marine Viral Single-chain Serine Palmitoyltransferase and Construction of Yeast and Mammalian Single-chain Chimera. Han, G., Gable, K., Yan, L., Allen, M.J., Wilson, W.H., Moitra, P., Harmon, J.M., Dunn, T.M. J. Biol. Chem. (2006) [Pubmed]
  20. Characterization of two novel yeast strains used in mediated biosensors for wastewater. Trosok, S.P., Luong, J.H., Juck, D.F., Driscoll, B.T. Can. J. Microbiol. (2002) [Pubmed]
WikiGenes - Universities