Rpl10, a ribosomal protein, is essential for ribosome function, playing a crucial role in protein translation. Ribosomes, where Rpl10 is located, are central to mRNA and protein quality control processes [2]. It is also involved in various signaling pathways, such as the JAK-STAT pathway in the context of T-cell acute lymphoblastic leukemia (T-ALL) [5].

In T-ALL, the R98S mutation in Rpl10 affects cellular proliferation, with cells accumulating reactive oxygen species, promoting mitochondrial dysfunction and reduced ATP levels [3]. These mutant leukemia cells survive high oxidative stress via increased IRES-mediated translation of BCL-2 [3]. Also, the R98S mutation enhances JAK-STAT signaling, as seen by overexpression of several Jak-Stat signaling proteins and hyper-activation of the pathway upon cytokine stimulation [5]. In pancreatic adenocarcinoma, the ufmylation of Rpl10 significantly increases cell proliferation and stemness, mainly due to higher expression of transcription factor KLF4 [1]. In plants like Nicotiana benthamiana and Arabidopsis, silencing or mutating Rpl10 compromises nonhost disease resistance, suggesting it positively regulates defence and translation-associated genes during nonhost pathogen infection [4].

In conclusion, Rpl10 is vital for ribosome-related functions and protein translation. Its study through genetic models, especially in diseases like T-ALL, pancreatic adenocarcinoma, and in understanding nonhost disease resistance in plants, has revealed its role in processes such as cell proliferation, stemness, and stress response. These findings contribute to a better understanding of disease mechanisms and may offer potential therapeutic targets.