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Gene Review

BMH2  -  14-3-3 family protein BMH2

Saccharomyces cerevisiae S288c

Synonyms: Protein BMH2, YD8557.08, YDR099W
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High impact information on BMH2

  • Here, we show that the S. cerevisiae 14-3-3 homologs BMH1 and BMH2 are not essential for viability or mating MAPK cascade signaling, but they are essential for pseudohyphal-development MAPK cascade signaling and other processes [1].
  • Moreover, Bmh1p and Bmh2p associate with Ste20p in vivo [1].
  • TOR inhibits expression of carbon-source-regulated genes by stimulating the binding of the transcriptional activators MSN2 and MSN4 to the cytoplasmic 14-3-3 protein BMH2 [2].
  • The inhibitory form of Mks1p is phosphorylated and complexed with the 14-3-3 proteins, Bmh1p and Bmh2p, which are also negative regulators of RS [3].
  • In addition, deletion of BMH2 rendered cells sensitive to citric acid [4].

Biological context of BMH2


Associations of BMH2 with chemical compounds

  • Multimeric presentation of the Arg-based signal from Kir6.2 on Pmp2p results in forward transport, which requires 14-3-3 proteins encoded in yeast by BMH1 and BMH2 in two isoforms [9].
  • We found that Yak1p interacted with Bmh1p and Bmh2p only in the presence of glucose [10].
  • Saccharomyces cerevisiae 14-3-3 proteins Bmh1 and Bmh2 participate in the process of catabolite inactivation of maltose permease [11].

Analytical, diagnostic and therapeutic context of BMH2


  1. 14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae. Roberts, R.L., Mösch, H.U., Fink, G.R. Cell (1997) [Pubmed]
  2. The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors. Beck, T., Hall, M.N. Nature (1999) [Pubmed]
  3. Retrograde signaling is regulated by the dynamic interaction between Rtg2p and Mks1p. Liu, Z., Sekito, T., Spírek, M., Thornton, J., Butow, R.A. Mol. Cell (2003) [Pubmed]
  4. Evidence of a new role for the high-osmolarity glycerol mitogen-activated protein kinase pathway in yeast: regulating adaptation to citric acid stress. Lawrence, C.L., Botting, C.H., Antrobus, R., Coote, P.J. Mol. Cell. Biol. (2004) [Pubmed]
  5. Regulation of transcription by Saccharomyces cerevisiae 14-3-3 proteins. Bruckmann, A., Steensma, H.Y., Teixeira De Mattos, M.J., Van Heusden, G.P. Biochem. J. (2004) [Pubmed]
  6. The 14-3-3 proteins positively regulate rapamycin-sensitive signaling. Bertram, P.G., Zeng, C., Thorson, J., Shaw, A.S., Zheng, X.F. Curr. Biol. (1998) [Pubmed]
  7. The Saccharomyces cerevisiae 14-3-3 protein Bmh2 is required for regulation of the phosphorylation status of Fin1, a novel intermediate filament protein. Mayordomo, I., Sanz, P. Biochem. J. (2002) [Pubmed]
  8. Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. Roth, D., Birkenfeld, J., Betz, H. FEBS Lett. (1999) [Pubmed]
  9. A multimeric membrane protein reveals 14-3-3 isoform specificity in forward transport in yeast. Michelsen, K., Mrowiec, T., Duderstadt, K.E., Frey, S., Minor, D.L., Mayer, M.P., Schwappach, B. Traffic (2006) [Pubmed]
  10. Yak1p, a DYRK family kinase, translocates to the nucleus and phosphorylates yeast Pop2p in response to a glucose signal. Moriya, H., Shimizu-Yoshida, Y., Omori, A., Iwashita, S., Katoh, M., Sakai, A. Genes Dev. (2001) [Pubmed]
  11. Saccharomyces cerevisiae 14-3-3 proteins Bmh1 and Bmh2 participate in the process of catabolite inactivation of maltose permease. Mayordomo, I., Regelmann, J., Horak, J., Sanz, P. FEBS Lett. (2003) [Pubmed]
  12. The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in the yeast Saccharomyces cerevisiae and can be replaced by a plant homologue. van Heusden, G.P., Griffiths, D.J., Ford, J.C., Chin-A-Woeng, T.F., Schrader, P.A., Carr, A.M., Steensma, H.Y. Eur. J. Biochem. (1995) [Pubmed]
  13. The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307. Callejo, M., Alvarez, D., Price, G.B., Zannis-Hadjopoulos, M. J. Biol. Chem. (2002) [Pubmed]
  14. Self-association of the spindle pole body-related intermediate filament protein Fin1p and its phosphorylation-dependent interaction with 14-3-3 proteins in yeast. van Hemert, M.J., Deelder, A.M., Molenaar, C., Steensma, H.Y., van Heusden, G.P. J. Biol. Chem. (2003) [Pubmed]
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