bp(GO:"protein polyubiquitination")
In some other cases, the first ubiquitin moiety is conjugated to the substrate by one E3, while chain elongation is catalyzed by a different ligase, often termed E4 PubMed:14556719
One key take-home message is that many E3 ligases likely evolved to be processive, meaning that they can conjugate multiple ubiquitins onto a substrate before it is released from enzyme PubMed:24457024
In this model,accumulation of an Hsp70–substrate complex (either via treatment with chemical inhibitors or because of intrinsic properties of the substrate) might allow enough time for a degradation factor (e.g., CHIP) to bind and facilitate polyubiquitination. PubMed:21882945
An E4 enzyme catalyzes the polyubiquitination of the target substrate that is bound to the E2–E3 complexes PubMed:22908190
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
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.