ReviewCurrent genetics2017
Hsp90 mediates the crosstalk between galactose metabolism and cell morphology pathways in yeast.
Review in Current genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Galactose Inhibits the Translation of Erg1 that Enhances the Antifungal Activities of Azoles AgainstAntibiotics (Basel, Switzerland) · 2025Article
- Nucleotide exchange is sufficient for Hsp90 functions in vivo.Nature communications · 2023Article
- Article
- Genome sequence and transcriptome profiles of pathogenic fungusComputational and structural biotechnology journal · 2021Article
- Novel insights into molecular chaperone regulation of ribonucleotide reductase.Current genetics · 2019Review
- How does Hsp90 function in RNAi-dependent heterochromatin assembly?Current genetics · 2019Review
- Branching the Tel2 pathway for exact fit on phosphatidylinositol 3-kinase-related kinases.Current genetics · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Galactose metabolism in the yeast Saccharomyces cerevisiae is carried out by a specialized GAL pathway consisting of structural and regulatory proteins. It is known that cells with unbalanced Gal proteins accumulate toxic metabolic intermediates and exhibit severe growth defects. Recently, we found that the molecular chaperone Hsp90 controls the abundance of multiple Gal proteins, possibly to prevent these defects. Hsp90 regulates various cellular processes including cell morphology in response to environmental cues. Yeast cells are known to resort to filamentous growth upon exposure to galactose or other environmental stresses. Our previous and current findings support the "Hsp90 titration model" of Hsp90 buffering, which links the cell morphology and galactose pathways. Our results suggest that, when a large proportion of Hsp90 molecules are used to help Gal proteins, the Hsp90 client proteins in cell morphology pathways are left unattended, leading to filamentous growth. It remains unclear whether this phenomenon serves any biological function or simply reflects a cellular constraint. Nonetheless, it provides an alternative explanation why the GAL pathway is degenerated in some yeast species.
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Registered trials
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