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Gene Review

GSC2  -  1,3-beta-glucan synthase GSC2

Saccharomyces cerevisiae S288c

Synonyms: 1,3-beta-D-glucan-UDP glucosyltransferase, 1,3-beta-glucan synthase component GSC2, FK506 sensitivity protein 2, FKS2, GLS2, ...
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Disease relevance of GSC2

  • On the other hand, reverse substitution of the corresponding amino acid of Fks2p (I1355K) resulted in loss of hypersensitivity to aerothricin3 [corrected] [1].

High impact information on GSC2

  • However, transcription of PMR2 and PMC1 was activated by only a subset of the treatments that activated FKS2 transcription [2].
  • Moreover, the calcineurin-dependent transcriptional induction of FKS2 in response to Ca2+, alpha-factor, and Na+ was found to require CRZ1 [2].
  • We describe new components of a calcineurin-mediated response in yeast, the Ca2+-induced transcriptional activation of FKS2, which encodes a beta-1,3 glucan synthase [2].
  • A 24-bp region of the FKS2 promoter was defined as sufficient to confer calcineurin-dependent transcriptional induction on a minimal promoter in response to Ca2+ and was named CDRE (for calcineurin-dependent response element) [2].
  • We find that 1,3-beta-glucan synthase activity is elevated in smk1 mutants, suggesting that SMK1 negatively regulates GSC2 [3].

Biological context of GSC2


Anatomical context of GSC2

  • Moreover, FKS2 is also highly induced in response to pheromone in a calcineurin-dependent manner, suggesting that FKS2 may also play a role in the remodeling of the cell wall during the mating process [6].
  • The Gtb1 protein was shown to be a soluble glycoprotein (96-102 kDa) localized to the endoplasmic reticulum lumen where it was present in a complex together with the yeast alpha-subunit homologue Gls2p [7].

Associations of GSC2 with chemical compounds

  • We analysed Fks1p and Fks2p in beta-1,6-glucan deficient mutants and found that they were mislocalized and that the mutants had reduced in vitro glucan synthase activity, possibly contributing to the observed beta-1,6-glucan defects [4].
  • In addition, eight out of 12 fks1ts fks2 delta mutants had altered beta-glucan levels at the permissive temperature: the partial killer resistant FKS1F1258Y N1520D allele was severely affected in both polymers and displayed a 55% reduction in beta-1,6-glucan, while the in vitro hyperactive allele FKS1T605I M761T increased both beta-glucan levels [4].
  • Induction of FKS2 expression in response to pheromone, CaCl2, or loss of FKS1 function requires the Ca2+/calmodulin-dependent protein phosphatase calcineurin [8].
  • These results suggest that the 1355th isoleucine of Fks2p plays a key role in aerothricin3 [corrected] sensitivity [1].
  • Thus, although Gls2p is sufficient for cleavage of the penultimate glucose residue, Gtb1p is essential for cleavage of the final glucose [7].

Other interactions of GSC2

  • Thus, the sensitivity of fks1 mutants to these drugs can be explained by the calcineurin-dependent transcription of FKS2 [6].
  • Expression of FKS2 from the heterologous ADH1 promoter results in FK506-resistant growth [6].
  • Yeast GS is composed of a putative catalytic subunit encoded by FKS1 and FKS2 and a regulatory subunit encoded by RHO1 [9].
  • Integration of the glucan interaction network with the caspofungin data indicates an overlapping set of genes involved in FKS2 regulation, compensatory chitin synthesis, protein mannosylation, and the PKC1-dependent cell integrity pathway [10].
  • With the exception of PHO89 and FKS2, none of the genes induced by Congo Red was up-regulated in a slt2 strain [11].

Analytical, diagnostic and therapeutic context of GSC2

  • In order to identify essential amino acid residues responsible for the sensitivity, each of the 10 non-conserved amino acids of Fks1p was substituted into the corresponding amino acid of Fks2p by site-directed mutagenesis [1].


  1. Differential sensitivity between Fks1p and Fks2p against a novel beta -1,3-glucan synthase inhibitor, aerothricin3 [corrected]. Kondoh, O., Takasuka, T., Arisawa, M., Aoki, Y., Watanabe, T. J. Biol. Chem. (2002) [Pubmed]
  2. Calcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeast. Stathopoulos, A.M., Cyert, M.S. Genes Dev. (1997) [Pubmed]
  3. The Smk1p MAP kinase negatively regulates Gsc2p, a 1,3-beta-glucan synthase, during spore wall morphogenesis in Saccharomyces cerevisiae. Huang, L.S., Doherty, H.K., Herskowitz, I. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  4. Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae. Dijkgraaf, G.J., Abe, M., Ohya, Y., Bussey, H. Yeast (2002) [Pubmed]
  5. Antifungal activity in Saccharomyces cerevisiae is modulated by calcium signalling. Edlind, T., Smith, L., Henry, K., Katiyar, S., Nickels, J. Mol. Microbiol. (2002) [Pubmed]
  6. Differential expression and function of two homologous subunits of yeast 1,3-beta-D-glucan synthase. Mazur, P., Morin, N., Baginsky, W., el-Sherbeini, M., Clemas, J.A., Nielsen, J.B., Foor, F. Mol. Cell. Biol. (1995) [Pubmed]
  7. Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. Wilkinson, B.M., Purswani, J., Stirling, C.J. J. Biol. Chem. (2006) [Pubmed]
  8. Temperature-induced expression of yeast FKS2 is under the dual control of protein kinase C and calcineurin. Zhao, C., Jung, U.S., Garrett-Engele, P., Roe, T., Cyert, M.S., Levin, D.E. Mol. Cell. Biol. (1998) [Pubmed]
  9. Dissection of upstream regulatory components of the Rho1p effector, 1,3-beta-glucan synthase, in Saccharomyces cerevisiae. Sekiya-Kawasaki, M., Abe, M., Saka, A., Watanabe, D., Kono, K., Minemura-Asakawa, M., Ishihara, S., Watanabe, T., Ohya, Y. Genetics (2002) [Pubmed]
  10. Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a synthetic interaction network and altered sensitivity to caspofungin. Lesage, G., Sdicu, A.M., Ménard, P., Shapiro, J., Hussein, S., Bussey, H. Genetics (2004) [Pubmed]
  11. The global transcriptional response to transient cell wall damage in Saccharomyces cerevisiae and its regulation by the cell integrity signaling pathway. García, R., Bermejo, C., Grau, C., Pérez, R., Rodríguez-Peña, J.M., Francois, J., Nombela, C., Arroyo, J. J. Biol. Chem. (2004) [Pubmed]
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