HTRA proteases: regulated proteolysis in protein quality control

Nat Rev Mol Cell Biol. 2011 Mar;12(3):152-62. doi: 10.1038/nrm3065. Epub 2011 Feb 16.


Controlled proteolysis underlies a vast diversity of protective and regulatory processes that are of key importance to cell fate. The unique molecular architecture of the widely conserved high temperature requirement A (HTRA) proteases has evolved to mediate critical aspects of ATP-independent protein quality control. The simple combination of a classic Ser protease domain and a carboxy-terminal peptide-binding domain produces cellular factors of remarkable structural and functional plasticity that allow cells to rapidly respond to the presence of misfolded or mislocalized polypeptides.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Enzyme Activation
  • Humans
  • Models, Biological
  • Models, Molecular
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • PDZ Domains
  • Photosynthesis
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Serine Proteases / chemistry
  • Serine Proteases / genetics
  • Serine Proteases / metabolism*
  • Temperature


  • Bacterial Proteins
  • Molecular Chaperones
  • Plant Proteins
  • Serine Proteases