title: HTRA proteases: regulated proteolysis in protein quality control.
abstract: 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.
authors.affiliation: Research Institute of Molecular Pathology, Dr. Bohrgasse 7, A-1030 Vienna, Austria. tim.clausen@imp.ac.at
authors.forename: Tim
authors.initials: T
authors.lastname: Clausen
authors.forename: Markus
authors.initials: M
authors.lastname: Kaiser
authors.forename: Robert
authors.initials: R
authors.lastname: Huber
authors.forename: Michael
authors.initials: M
authors.lastname: Ehrmann
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004789:Enzyme Activation; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D054731:PDZ Domains; D010788:Photosynthesis; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D057057:Serine Proteases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones; D010940:Plant Proteins; D057057:Serine Proteases