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The HtrA family of proteases: Implications for protein composition and cell fate

被引：542
作者：
Clausen, T
Southan, C
Ehrmann, M
机构：
[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany
[2] Cardiff Univ, Sch Biosci, Cardiff CF10 3US, S Glam, Wales
[3] Oxford GlycoSci UK Ltd, Abingdon OX14 4RY, Oxon, England
来源：
MOLECULAR CELL | 2002年 / 10卷 / 03期
基金：
英国生物技术与生命科学研究理事会;
关键词：
D O I：
10.1016/S1097-2765(02)00658-5
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Cells precisely monitor the concentration and functionality of each protein for optimal performance. Protein quality control involves molecular chaperones, folding catalysts, and proteases that are often heat shock proteins. One quality control factor is HtrA, one of a new class of oligomeric serine proteases. The defining feature of the HtrA family is the combination of a catalytic domain with at least one C-terminal PDZ domain. Here, we discuss the properties and roles of this ATP-independent protease chaperone system in protein metabolism and cell fate.
引用
收藏
页码：443 / 455
页数：13
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