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Gene Review

BMH1  -  14-3-3 family protein BMH1

Saccharomyces cerevisiae S288c

Synonyms: Protein BMH1, YER177W
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Disease relevance of BMH1

  • These genes include approximately 60 elements that could be linked to the reported phenotypes of the bmhDelta mutant (e.g., accumulation of glycogen and hypersensitivity to environmental stress) and/or could be the potential downstream targets of interacting partners of Bmh1/2p such as Msn2p and Rtg3p [1].

High impact information on BMH1

  • 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 [2].
  • Three alleles of BMH1 encode proteins defective for FG(TyA)-lacZ signaling and association with Ste20p, yet these alleles complement other 14-3-3 functions [2].
  • We found that Yak1p interacted with Bmh1p and Bmh2p only in the presence of glucose [3].
  • HOG1 negatively regulated the expression of a number of proteins in response to citric acid stress, including Bmh1p [4].
  • Evidence suggests that BMH1 is induced by citric acid to counteract the effect of amino acid starvation [4].

Biological context of BMH1

  • Mutations in PIO3 (unidentified) cause a weaker Pio phenotype, enhanced by a null mutation in BMH1, one of two yeast 14-3-3 proteins [5].
  • We propose that function of BMH1 as a negative regulator of SOU1 contributes to a general cellular homeostasis [6].
  • This is a first report on the role of the C. albicans essential gene BMH1 as a negative regulator of the utilization of secondary carbon source in yeast, which further substantiates the involvement of 14-3-3 proteins in diverse functions [6].
  • Although the exact mechanism of the interaction between BMH1 and SOU1 is not known, it is clear that the control is based on the ratio of gene copy number, and that BMH1 does not control the loss of chromosome 5, the major mechanism producing Sou+ mutants [6].
  • BMH1 and BMH2 encode homologs of the 14-3-3 signal transduction proteins [7].

Associations of BMH1 with chemical compounds

  • The present work compares the transcriptomic and proteomic profiles of the wild type and a BMH1/2-deficient S. cerevisiae mutant (bmhDelta) using DNA microarrays and two-dimensional polyacrylamide gel electrophoresis [1].
  • We report here another negative regulator of L-sorbose utilization, an orthologue of the Saccharomyces cerevisiae BMH1 gene, which encodes the evolutionarily conserved protein 14-3-3 [6].
  • In contrast to strains with an intact or a disrupted BMH1 gene, strains with the BMH1 gene on multicopy plasmids hardly grew on media with acetate or glycerol as carbon source [8].
  • 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].
  • Importantly, >30% of the identified genes (71 genes) were found to be associated with carbon (C) and nitrogen (N) metabolism and transport, thereby suggesting that Bmh1/2p may play a major role in the regulation of C/N-responsive cellular processes [1].

Physical interactions of BMH1

  • Mks1p is negatively regulated by binding to Rtg2p and positively regulated when bound to Bmh1/2p [10].
  • Here we show that the Reg1-interacting proteins Bmh1, Bmh2, Ssb1, and Ssb2 have roles in glucose repression [11].

Other interactions of BMH1

  • Grr1p polyubiquitinates Mks1p not bound to either Rtg2p or to Bmh1/2p, targeting it for degradation [10].
  • Unexpectedly, a fraction of the purified tagged PMA2 associated with the two yeast 14-3-3 regulatory proteins, BMH1 and BMH2 [12].
  • The Reg1-interacting proteins, Bmh1, Bmh2, Ssb1, and Ssb2, have roles in maintaining glucose repression in Saccharomyces cerevisiae [11].
  • Here, we describe the interaction of the Fin1 protein with the 14-3-3 proteins Bmh1p and Bmh2p in more detail [13].
  • We identified 14-3-3 as a Dyrk1A interacting protein, which is consistent with the previous finding of the interaction between the yeast orthologues Yak1p and Bmh1/2p [14].

Analytical, diagnostic and therapeutic context of BMH1

  • The essentiality of C. albicans BMH1 was confirmed by a PCR disruption technique [15].
  • The 14-3-3 gene in Candida albicans (BMH1) was identified using a novel adherence assay and differential display RT-PCR [15].
  • In agreement with the finding of an association of Bmh1p and Bmh2p with ARS307, another immunoprecipitation experiment using 2D3, an anti-cruciform DNA monoclonal antibody, revealed the presence of cruciform-containing DNA in ARS307 [16].
  • Surface plasmon resonance analysis showed that Fin1p has a higher affinity for Bmh2p than for Bmh1p (K(D) 289 versus 585 nm) [13].


  1. Transcriptomic and proteomic analysis of a 14-3-3 gene-deficient yeast. Ichimura, T., Kubota, H., Goma, T., Mizushima, N., Ohsumi, Y., Iwago, M., Kakiuchi, K., Shekhar, H.U., Shinkawa, T., Taoka, M., Ito, T., Isobe, T. Biochemistry (2004) [Pubmed]
  2. 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]
  3. 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]
  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. Yeast genes controlling responses to topogenic signals in a model transmembrane protein. Tipper, D.J., Harley, C.A. Mol. Biol. Cell (2002) [Pubmed]
  6. Role of the 14-3-3 protein in carbon metabolism of the pathogenic yeast Candida albicans. Wang, Y.K., Das, B., Huber, D.H., Wellington, M., Kabir, M.A., Sherman, F., Rustchenko, E. Yeast (2004) [Pubmed]
  7. 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]
  8. Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors. van Heusden, G.P., Wenzel, T.J., Lagendijk, E.L., de Steensma, H.Y., van den Berg, J.A. FEBS Lett. (1992) [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. A novel degron-mediated degradation of the RTG pathway regulator, Mks1p, by SCFGrr1. Liu, Z., Spírek, M., Thornton, J., Butow, R.A. Mol. Biol. Cell (2005) [Pubmed]
  11. The Reg1-interacting proteins, Bmh1, Bmh2, Ssb1, and Ssb2, have roles in maintaining glucose repression in Saccharomyces cerevisiae. Dombek, K.M., Kacherovsky, N., Young, E.T. J. Biol. Chem. (2004) [Pubmed]
  12. A plant plasma membrane H+-ATPase expressed in yeast is activated by phosphorylation at its penultimate residue and binding of 14-3-3 regulatory proteins in the absence of fusicoccin. Maudoux, O., Batoko, H., Oecking, C., Gevaert, K., Vandekerckhove, J., Boutry, M., Morsomme, P. J. Biol. Chem. (2000) [Pubmed]
  13. 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]
  14. Regulation of Dyrk1A kinase activity by 14-3-3. Kim, D., Won, J., Shin, D.W., Kang, J., Kim, Y.J., Choi, S.Y., Hwang, M.K., Jeong, B.W., Kim, G.S., Joe, C.O., Chung, S.H., Song, W.J. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  15. The Candida albicans 14-3-3 gene, BMH1, is essential for growth. Cognetti, D., Davis, D., Sturtevant, J. Yeast (2002) [Pubmed]
  16. 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]
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