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

• Steady-state mRNA levels of 60 open reading frames were increased more than 2.0-fold in the bmh2 mutant, whereas those of 78 open reading frames were decreased more than 2.0-fold [5].
• RESULTS: We isolated two Saccharomyces cerevisiae genes, BMH1 and BMH2, as multicopy suppressors of the growth-inhibitory phenotype caused by rapamycin in budding yeast [6].
• BMH1 and BMH2 encode homologs of the 14-3-3 signal transduction proteins [6].
• The Saccharomyces cerevisiae 14-3-3 protein Bmh2 is required for regulation of the phosphorylation status of Fin1, a novel intermediate filament protein [7].
• Cells overexpressing the carboxy-terminal region of Bmh2p failed to polarize vesicular transport although bulk exocytosis remained unaffected and showed a disrupted actin cytoskeleton [8].

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

• Using the polymerase chain reaction method, we have isolated a second yeast gene encoding a 14-3-3 protein (BMH2) [12].
• 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 [13].
• Surface plasmon resonance analysis showed that Fin1p has a higher affinity for Bmh2p than for Bmh1p (K(D) 289 versus 585 nm) [14].

References