On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60

Cell Stress Chaperones. Summer 2006;11(2):116-28. doi: 10.1379/csc-144r.1.

Abstract

The heat shock chaperones mortalin/mitochondrial heat shock protein 70 (mtHsp70) and Hsp60 are found in multiple subcellular sites and function in the folding and intracellular trafficking of many proteins. The chaperoning activity of these 2 proteins involves different structural and functional mechanisms. In spite of providing an excellent model for an evolutionarily conserved molecular "brotherhood", their individual functions, although overlapping, are nonredundant. As they travel to various locations, both chaperones acquire different binding partners and exert a more divergent involvement in tumorigenesis, cellular senescence, and immunology. An understanding of their functional biology may lead to novel designing and development of therapeutic strategies for cancer and aging.

Publication types

  • Review

MeSH terms

  • Animals
  • Apoptosis / physiology
  • Chaperonin 60 / metabolism*
  • Chaperonin 60 / physiology
  • HSP70 Heat-Shock Proteins / metabolism*
  • HSP70 Heat-Shock Proteins / physiology
  • Heat-Shock Response / physiology
  • Humans
  • Mitochondrial Proteins / metabolism
  • Mitochondrial Proteins / physiology
  • Models, Biological
  • Molecular Chaperones / metabolism*
  • Molecular Chaperones / physiology
  • Neoplasms / metabolism
  • Neoplasms / physiopathology

Substances

  • Chaperonin 60
  • HSP70 Heat-Shock Proteins
  • Mitochondrial Proteins
  • Molecular Chaperones
  • mortalin