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Molecular chaperones and the cytoskeleton

P Liang1, T H MacRae

  • 1Department of Biology, Dalhousie University, Halifax, NS, Canada.

Journal of Cell Science
|July 1, 1997
PubMed
Summary

Heat shock proteins act as molecular chaperones, aiding protein folding and cellular processes. This review explores their crucial, cooperative roles in forming and maintaining the eukaryotic cytoskeleton.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Heat shock proteins (HSPs) are synthesized under stress and constitutively.
  • HSPs function as molecular chaperones, influencing protein structure and cellular processes.
  • They are classified into families: HSP100, 90, 70, 60, and small HSPs/alpha-crystallins.

Purpose of the Study:

  • To review the relationship between molecular chaperones and the cytoskeleton.
  • To highlight the roles of HSPs in cytoskeletal protein folding, assembly, and protection.

Main Methods:

  • Literature review of emerging research on HSPs and the cytoskeleton.
  • Analysis of studies identifying specific HSP-cytoskeletal interactions and functions.

Main Results:

  • The TCP-1 complex is identified as the eukaryotic cytoplasmic chaperonin for cytoskeletal proteins like tubulin and actin.
  • TCP-1 complex is involved in microtubule nucleation at the centrosome.
  • HSP70 and HSP90 interact with microtubules, while small HSPs interact with microfilaments and intermediate filaments, modulating their assembly and providing protection.

Conclusions:

  • Molecular chaperones, including HSPs, play diverse yet cooperative roles in the formation and function of the eukaryotic cytoskeleton.
  • HSPs protect cytoskeletal components from stress and influence their dynamic assembly processes.

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