The Roles of Molecular Chaperones in Regulating Cell Metabolism

Fluctuations in nutrient and biomass availability, often as a result of disease, impart metabolic challenges that must be overcome in order to sustain cell survival and promote proliferation. Cells adapt to these environmental changes and stresses by adjusting their metabolic networks through a series of regulatory mechanisms. Our understanding of these rewiring events has largely been focused on those genetic transformations that alter protein expression and the biochemical mechanisms that change protein behavior, such as post-translational modifications and metabolite-based allosteric modulators. Mounting evidence suggests that a class of proteome surveillance proteins called molecular chaperones also can influence metabolic processes. Here, we summarize several ways the Hsp90 and Hsp70 chaperone families act on human metabolic enzymes and their supramolecular assemblies to change enzymatic activities and metabolite flux. We further highlight how these chaperones can assist in the translocation and degradation of metabolic enzymes. Collectively, these studies provide a new view for how metabolic processes are regulated to meet cellular demand and inspire new avenues for therapeutic intervention.

Note: For access to the metabolic enzyme interaction map shown in Figure 2, please consult the Hsp90-Metabolic Enzyme Network.cys README file first.

Citation

Pedley, Anthony; Binder, Matthew (2023). The Roles of Molecular Chaperones in Regulating Cell Metabolism [Data set]. Scholarsphere.

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Work Title The Roles of Molecular Chaperones in Regulating Cell Metabolism
Access
Open Access
Creators
  1. Anthony Pedley
  2. Matthew Binder
Keyword
  1. Cellular metabolism
  2. Metabolons
  3. Molecular chaperones
  4. Protein degradation
  5. Protein folding
  6. Supramolecular complexes
License CC BY 4.0 (Attribution)
Work Type Dataset
Acknowledgments
  1. Huck Institutes of the Life Sciences (Huck Innovative and Transformative Seed Fund Grant to AMP)
Publisher
  1. FEBS Letters
Publication Date July 2023
Publisher Identifier (DOI)
  1. 10.1002/1873-3468.14682
Related URLs
Deposited August 05, 2023

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Version 1
published

  • Created
  • Updated
  • Updated Acknowledgments Show Changes
    Acknowledgments
    • Huck Institutes of the Life Sciences (Huck Innovative and Transformative Seed Fund Grant to AMP)
  • Added Creator Anthony Pedley
  • Added Creator Matthew Binder
  • Added Fig1_Chaperone Cycles.tiff
  • Added Fig2_Network.tiff
  • Added Fig3_Complexes.tiff
  • Added Fig4_CMA.tiff
  • Added Hsp90-Metabolic Enzyme Network.cys
  • Updated Keyword, Publisher, Related URLs, and 1 more Show Changes
    Keyword
    • cellular metabolism, metabolons, molecular chaperones, protein degradation, protein folding, supramolecular complexes
    Publisher
    • FEBS Letters
    Related URLs
    • https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14682
    License
    • https://creativecommons.org/licenses/by/4.0/
  • Published
  • Updated Keyword Show Changes
    Keyword
    • cellular metabolism, metabolons, molecular chaperones, protein degradation, protein folding, supramolecular complexes
    • Cellular metabolism, Metabolons, Molecular chaperones, Protein degradation, Protein folding, Supramolecular complexes
  • Updated

Version 2
published

  • Created
  • Updated Description Show Changes
    Description
    • Fluctuations in nutrient and biomass availability, often as a result of disease, impart metabolic challenges that must be overcome in order to sustain cell survival and promote proliferation. Cells adapt to these environmental changes and stresses by adjusting their metabolic networks through a series of regulatory mechanisms. Our understanding of these rewiring events has largely been focused on those genetic transformations that alter protein expression and the biochemical mechanisms that change protein behavior, such as post-translational modifications and metabolite-based allosteric modulators. Mounting evidence suggests that a class of proteome surveillance proteins called molecular chaperones also can influence metabolic processes. Here, we summarize several ways the Hsp90 and Hsp70 chaperone families act on human metabolic enzymes and their supramolecular assemblies to change enzymatic activities and metabolite flux. We further highlight how these chaperones can assist in the translocation and degradation of metabolic enzymes. Collectively, these studies provide a new view for how metabolic processes are regulated to meet cellular demand and inspire new avenues for therapeutic intervention.
    • Fluctuations in nutrient and biomass availability, often as a result of disease, impart metabolic challenges that must be overcome in order to sustain cell survival and promote proliferation. Cells adapt to these environmental changes and stresses by adjusting their metabolic networks through a series of regulatory mechanisms. Our understanding of these rewiring events has largely been focused on those genetic transformations that alter protein expression and the biochemical mechanisms that change protein behavior, such as post-translational modifications and metabolite-based allosteric modulators. Mounting evidence suggests that a class of proteome surveillance proteins called molecular chaperones also can influence metabolic processes. Here, we summarize several ways the Hsp90 and Hsp70 chaperone families act on human metabolic enzymes and their supramolecular assemblies to change enzymatic activities and metabolite flux. We further highlight how these chaperones can assist in the translocation and degradation of metabolic enzymes. Collectively, these studies provide a new view for how metabolic processes are regulated to meet cellular demand and inspire new avenues for therapeutic intervention.
    • Note: For access to the metabolic enzyme interaction map shown in Figure 2, please consult the Hsp90-Metabolic Enzyme Network.cys README file first.
  • Added README_Hsp90-Metabolic Enzyme Network.txt
  • Published
  • Updated