Faculty Opinions recommendation of The polycomb protein Pc2 is a SUMO E3.

By Andrew D. Sharrocks. 2003

605 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/b594bcb24d68d69819ed9f9204f977f2d5f27996

Citations in the corpus

• Polycomb silencers control cell fate, development and cancer (2006, unknown): “Additionally, BMI1 contains a SUMO consensus site and interacts with PC2, a Polycomb group protein that has SUMO E3 ligase activit”
• Insights in Post-Translational Modifications: Ubiquitin and SUMO (2022, unknown): “Other SUMO E3 enzymes Pc2/CBX4 SUMO1 CtBP Polycomb bodies [115]”
• Concepts in sumoylation: a decade on (2007, unknown): “Overexpression of Pc2 results in enhanced CtBP sumoylation, and recombinant Pc2 enhances CtBP1 and CtBP2 modification in vitro”
• SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? (2004, unknown): “Although recombinant E1, E2, and SUMO are sufficient for SUMOylation of the transcriptional corepressor CtBP-1 in vitro, expression of Pc2 increased SUMO modification of CtBP-1 in vivo (Kagey et al. 2003).”
• Sumoylation: a regulatory protein modification in health and disease. (2013, unknown): “Among these is the human polycomb protein Pc2/CBX4, a component of the multimeric polycomb repressive complex 1 (PRC1) that stimulates CtBP1 sumoylation in vitro and in vivo (71).”
• Biogenesis and Function of Nuclear Bodies (2011, unknown): “The human PcG protein Pc2 has been demonstrated to act as a SUMO E3 ligase by bringing the SUMO E2 (Ubc9) and the substrates (CtBP and CTCF) together, thereby making PcG bodies sumoylation centers [105, 106] (Figure 3c).”
• Nuclear and unclear functions of SUMO (2003, unknown): “Although the SUMO E3 enzymes are able to undergo a process akin to the ubiquitin E3 'substrate-independent modification', in that PIAS proteins, RanBP2 and Pc2 are all sumoylated themselve”