Feeding the machine: mechanisms of proteasome-catalyzed degradation of ubiquitinated proteins

被引:28
作者
Crews, CM
机构
[1] Yale Univ, Dept Mol Cell & Dev Biol, New Haven, CT 06520 USA
[2] Yale Univ, Dept Chem, New Haven, CT 06520 USA
[3] Yale Univ, Dept Pharmacol, New Haven, CT 06520 USA
关键词
D O I
10.1016/j.cbpa.2003.08.002
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
The proteasome plays a role in a myriad of intracellular processes from cell-cycle control to antigen presentation. Central to these processes is the targeting of selected proteins for proteasomal degradation via their conjugation to ubiquitin. The mechanisms by which the ubiquitin-dependent proteasomal proteolysis occurs can be divided into four steps: first, substrate protein recognition by its cognate E3 ubiquitin ligase; second, polyubiquitinated protein substrate recruitment to the proteasome; third, protein substrate deubiquitination; and four, proteolytic chamber pore opening/substrate translocation followed by proteolysis. Recent advances include the identification of novel E3 ubiquitin ligase recognition determinants, a new isopeptidase activity, and a better understanding of how the proteasome's axial channels are gated.
引用
收藏
页码:534 / 539
页数:6
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