HTRA proteases: regulated proteolysis in protein quality control

被引：368

作者：

Clausen, Tim ^{[1
]}

Kaiser, Markus ^{[2
]}

Huber, Robert ^{[2
,3
,4
]}

Ehrmann, Michael ^{[2
,4
]}

机构：

[1] Res Inst Mol Pathol IMP, A-1030 Vienna, Austria

[2] Univ Duisburg Essen, Ctr Med Biotechnol, Fac Biol, D-45117 Essen, Germany

[3] Max Planck Inst Biochem, D-82152 Martinsried, Germany

[4] Cardiff Univ, Sch Biosci, Cardiff CF10 3US, S Glam, Wales

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2011年 / 12卷 / 03期

关键词：

HIGH-TEMPERATURE REQUIREMENT; AMYLOID PRECURSOR PROTEIN; IGF-BINDING PROTEINS; ENVELOPE-STRESS-RESPONSE; GROWTH-FACTOR IGF; SERINE-PROTEASE; ESCHERICHIA-COLI; PHOTOSYSTEM-II; PDZ DOMAIN; CRYSTAL-STRUCTURE;

D O I：

10.1038/nrm3065

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

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页码：152 / 162

页数：11

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