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Here, we analyzed the impact of the ubiquitin\u2010like protein SUMO on the RPL11\u2010mouse double\u2010minute 2 homolog\u2010p53 signaling. We show that small ubiquitin\u2010related modifier (SUMO)1 and SUMO2 covalently modify RPL11. We find that SUMO negatively modulates the conjugation of the ubiquitin\u2010like protein neural precursor cell\u2010expressed developmentally downregulated 8 (NEDD8) to RPL11 and promotes the translocation of the RP outside of the nucleoli. Moreover, the SUMO\u2010conjugating enzyme, Ubc9, is required for RPL11\u2010mediated activation of p53. SUMOylation of RPL11 is triggered by ribosomal stress, as well as by alternate reading frame protein upregulation. Collectively, our data identify SUMO protein conjugation to RPL11 as a new regulator of the p53\u2010mediated cellular response to different types of stress and reveal a previously unknown SUMO\u2010NEDD8 interplay.\u2014El Motiam, A., Vidal, S., de la Cruz\u2010Herrera, C. F., Da Silva\u2010\u00c1lvarez, S., Baz\u2010Mart\u00ednez, M., Seoane, R., Vidal, A., Rodr\u00edguez, M. S., Xirodimas, D. P., Carvalho, A. S., Beck, H. C., Matthiesen, R., Collado, M., Rivas, C. Interplay between SUMOylation and NEDDylation regulates RPL11 localization and function. 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