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Gene Review

LCB2  -  serine C-palmitoyltransferase LCB2

Saccharomyces cerevisiae S288c

Synonyms: D4246, Long chain base biosynthesis protein 2, SCS1, SPT 2, Serine palmitoyltransferase 2, ...
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Disease relevance of LCB2


High impact information on LCB2

  • Here we demonstrate that overproduction in Saccharomyces cerevisiae requires expression of LCB1, a previously isolated yeast gene, and LCB2, the isolation and characterization of which we describe [3].
  • 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 [2].
  • The TSC1 gene was recently identified and codes for hamartin, a novel protein with no significant homology to tuberin or any other known vertebrate protein [4].
  • Furthermore, mutations in this lysine and in a histidine residue that is also predicted to be important for pyridoxal 5'-phosphate binding to Lcb2p also dominantly inactivate SPT similar to the hereditary sensory neuropathy type 1-like mutations in Lcb1p [1].
  • Tuberous sclerosis is caused by mutations to either the TSC1 or TSC2 tumor suppressor gene [5].

Biological context of LCB2

  • Northern blot analysis of mRNA isolated from various mouse tissues revealed that the tissue distribution of both LCB1 and LCB2 messengers followed a similar pattern [6].
  • We conclude that the Lcb- phenotype of these mutants results from a missing or defective SPT, an activity controlled by both the LCB1 and LCB2 genes [7].
  • Southern blot analysis and inspection of the complete Arabidopsis genome sequence database suggest that there is a second LCB2-like gene in Arabidopsis [8].
  • After transformation of an LCB2 gene expression cassette, several transformants that contained approximately five to seven copies of transforming DNA in the chromosome and exhibited about 50-fold increase in LCB2 mRNA relative to the wild type were identified [9].
  • Our data support a model in which Pas1 inhibits G1 arrest downstream of Tsc1 and Tsc2, linking nutrient uptake and cell cycle progression in yeast [2].

Anatomical context of LCB2

  • We isolated mammalian LCB1 cDNA homologs from mouse and Chinese hamster ovary (CHO) cells and an LCB2 cDNA homolog from CHO cells [6].
  • Taken together, these data suggest that in contrast to other members of the alpha-oxoamine synthases that are soluble homodimers, the Lcb1p and Lcb2p subunits of the SPT heterodimer may interact in the cytosol, as well as within the membrane and/or the lumen of the endoplasmic reticulum [10].

Associations of LCB2 with chemical compounds

  • Secondary phenotypes of the scs1 mutants indicate that SCS1 is required for serine palmitoyltransferase activity which catalyzes the first committed step in sphingolipid biosynthesis (palmitoyl-CoA + serine-->3-ketosphinganine+CoASH+CO2) [11].
  • Expression of these mutants confers resistance to canavanine and thialysine, phenotypes which are similar to phenotypes exhibited by cells lacking the Tsc1/Tsc2 complex that negatively regulates Rhb1 [12].
  • The mammalian LCB2 cDNAs provide valuable reagents for studying the Lcb2 subunit of SPT and for studying how ceramide synthesis is regulated [13].

Other interactions of LCB2

  • Lcb1p and Lcb2p remain tightly associated with each other and localize to the membrane in cells lacking Tsc3p [14].
  • Two other genes involved in sphingolipid biosynthesis (LCB2 and SUR2) were found to contain PDREs in their promoters and to be induced by the Pdr pathway [15].

Analytical, diagnostic and therapeutic context of LCB2

  • Sequence alignment and mutational analysis showed that the N-terminal domain of the viral protein most closely resembled the LCB2 subunit and the C-terminal domain most closely resembled the LCB1 subunit [16].
  • After isolation from a pulp mill wastewater treatment facility, two yeast strains, designated SPT1 and SPT2, were characterized and used in the development of mediated biochemical oxygen demand (BOD) biosensors for wastewater [17].


  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. 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]
  3. The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis. Nagiec, M.M., Baltisberger, J.A., Wells, G.B., Lester, R.L., Dickson, R.C. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  4. Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products. van Slegtenhorst, M., Nellist, M., Nagelkerken, B., Cheadle, J., Snell, R., van den Ouweland, A., Reuser, A., Sampson, J., Halley, D., van der Sluijs, P. Hum. Mol. Genet. (1998) [Pubmed]
  5. Identification and characterization of the interaction between tuberin and 14-3-3zeta. Nellist, M., Goedbloed, M.A., de Winter, C., Verhaaf, B., Jankie, A., Reuser, A.J., van den Ouweland, A.M., van der Sluijs, P., Halley, D.J. J. Biol. Chem. (2002) [Pubmed]
  6. 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]
  7. 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]
  8. Characterization of an Arabidopsis cDNA encoding a subunit of serine palmitoyltransferase, the initial enzyme in sphingolipid biosynthesis. Tamura, K., Mitsuhashi, N., Hara-Nishimura, I., Imai, H. Plant Cell Physiol. (2001) [Pubmed]
  9. 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]
  10. 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]
  11. 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]
  12. Identification of novel single amino acid changes that result in hyperactivation of the unique GTPase, Rheb, in fission yeast. Urano, J., Comiso, M.J., Guo, L., Aspuria, P.J., Deniskin, R., Tabancay, A.P., Kato-Stankiewicz, J., Tamanoi, F. Mol. Microbiol. (2005) [Pubmed]
  13. Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase. Nagiec, M.M., Lester, R.L., Dickson, R.C. Gene (1996) [Pubmed]
  14. 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]
  15. Differential regulation of ceramide synthase components LAC1 and LAG1 in Saccharomyces cerevisiae. Kolaczkowski, M., Kolaczkowska, A., Gaigg, B., Schneiter, R., Moye-Rowley, W.S. Eukaryotic Cell (2004) [Pubmed]
  16. 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]
  17. 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]
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