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Curr Opin Chem Biol. 2003 Oct;7(5):534-9.

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

Author information

1
Departments of Molecular, Cell and Developmental Biology, Yale University, PO Box 208103, New Haven, CT 06520-8130, USA. craig.crews@yale.edu

Abstract

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.

PMID:
14580555
[Indexed for MEDLINE]

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