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.
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Hartmann-Petersen, R., Gordon, C. Ubiquitin-proteasome system. CMLS, Cell. Mol. Life Sci. 61, 1589–1595 (2004). https://doi.org/10.1007/s00018-004-4132-x
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DOI: https://doi.org/10.1007/s00018-004-4132-x