Journal of Cancer Prevention : pISSN 2288-3649 / eISSN 2288-3657

Fig. 2.

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Fig. 2. Cross-talk between 26S and 20S proteasome under oxidative stress. The 26S proteasome degrades not only abnormally folded or damaged proteins but also fully folded proteins through ubiquitination. Under oxidative stress, however, the 19S regulatory particle that constitutes the 26S proteasome is dissociated from the 20S proteasome. The dissociated 20S proteasome mediates oxidized protein degradation. 19S regulatory particle is held by chaperone HSP70, and over time it binds to the 20S proteasome and is reassembled into 26S proteasome. Ub, ubiquitin.
Journal of Cancer Prevention 2018;23:153-61 https://doi.org/10.15430/JCP.2018.23.4.153
© 2018 Journal of Cancer Prevention