10. Concluding Remarks
It becomes increasingly evident that protein ubiquitination is closely linked to many aspects of the immune system and the E3 ubiquitin ligases play an important role in those processes via specific targeting of protein substrates. Gene database searching has indicated that there are several hundred E3 ubiquitin ligases, with the majority being RING finger-containing E3 ligases. It is conceivable that there will be very complicated interplay among the E3 ligases. Several E3 ligases may target the same substrate, or otherwise, one E3 ligase may target different substrates under diverse physiological conditions. In addition, the list of de-ubiquiting enzymes involved in immune regulation will increase in the near future. It has to be mentioned that biochemical and molecular approaches are still the main tools for identification of a substrate for a particular E3 ubiquitin ligase. The physiological relevance of such findings has to be correlated with genetic investigations. In any case, the field of research on protein ubiquitination in immune modulation will continue to be a hot topic in the years to come.
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Venuprasad, K. et al. (2006). Immune Regulation by Ubiquitin Conjugation. In: Tsoukas, C. (eds) Lymphocyte Signal Transduction. Advances in Experimental Medicine and Biology, vol 584. Springer, Boston, MA. https://doi.org/10.1007/0-387-34132-3_15
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