Abstract
The 26S proteasome is the multi-protein protease that recognizes and degrades ubiquitinylated substrates targeted for destruction by the ubiquitin pathway. In addition to the well-documented subunit organization of the 26S holoenzyme, it is clear that a number of other proteins transiently associate with the 26S complex. These transiently associated proteins confer a number of different roles such as substrate presentation, cleavage of the multi-ubiquitin chain from the protein substrate and turnover of misfolded proteins. Such activities are essential for the 26S proteasome to efficiently fulfill its intracellular function in protein degradation.
Original language | English |
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Journal | Cellular and molecular life sciences : CMLS |
Volume | 61 |
Issue number | 13 |
Pages (from-to) | 1589-95 |
Number of pages | 6 |
ISSN | 1420-682X |
DOIs | |
Publication status | Published - 2004 |