p(HGNC:PSMD14)
Thus, the binding of substrate to the 26S and its concomitant translocation into the 20S results in the activation of Rpn11 through a conformational change. PubMed:24457024
Second, Rpn11/Poh1 (also known as Psmd14) is a subunit in the 19S regulatory particle that cleaves the entire, intact ubiquitin chain from the protein substrate [71,72]. PubMed:24457024
This observation suggests that chain binding and cleavage from the protein substrate are tightly coordinated by the proteasome, and may help to prevent situations such as premature chain cleavage by Rpn11, which could result in the release of the substrate before it becomes actively engaged to the proteasome. PubMed:24457024
This activity promotes both the recycling of chains back into the free cellular pool of ubiquitin and creates space for the protein substrate to enter the 20S core. PubMed:24457024
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.