{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRecent studies have uncovered unexpected extra‐ribosomal functions for ribosomal proteins that not only affect protein synthesis but also impinge on the regulation of non‐coding RNAs. For example, mutations in ribosomal protein L24, as characterized in the Belly spot and tail (Bst) mouse, lead to defective splicing and ribosome biogenesis with consequent reductions in protein synthesis and cell proliferation, thereby influencing broader gene regulatory networks."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nComplementing these findings, investigations into mitochondrial dynamics have demonstrated that mOPA1—a dynamin GTPase—localizes to mitochondria and modulates their morphology, especially in neuronal and glial cells. Although mOPA1 primarily influences mitochondrial structure and function, such cellular perturbations can indirectly affect non‐coding RNA pathways by altering the metabolic and signaling environments that govern gene expression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nA particularly intriguing discovery has emerged regarding the regulation of primate-specific microRNAs. In a recent study, a short 150-base DNA sequence immediately upstream of a microRNA precursor (hsa-miR-608) was identified as an independent promoter element that robustly boosts its expression. Moreover, ribosomal protein L24 was found to bind this regulatory region and interact with the microprocessor complex protein DDX5 to inhibit microRNA processing. While the study focused on miR-608, these results suggest that similar extra-ribosomal mechanisms may regulate other primate-specific microRNAs, such as MIR4703. If MIR4703 falls within this regulatory network, it is plausible that its biogenesis is tightly controlled by factors like RPL24, thereby permitting fine-tuning of post-transcriptional gene expression programs involved in processes such as inflammation and cell differentiation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Edward R Oliver, Thomas L Saunders, Susan A Tarlé, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein L24 defect in belly spot and tail (Bst), a mouse Minute."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Development (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/dev.01268"}], "href": "https://doi.org/10.1242/dev.01268"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15289434"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15289434"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Martina Barkić, Sladana Crnomarković, Kristina Grabusić, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The p53 tumor suppressor causes congenital malformations in Rpl24-deficient mice and promotes their survival."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.01588-08"}], "href": "https://doi.org/10.1128/MCB.01588-08"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19273598"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19273598"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Takumi Misaka, Tomoyuki Miyashita, Yoshihiro Kubo "}, {"type": "b", "children": [{"type": "t", "text": "Primary structure of a dynamin-related mouse mitochondrial GTPase and its distribution in brain, subcellular localization, and effect on mitochondrial morphology."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109260200"}], "href": "https://doi.org/10.1074/jbc.M109260200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11847212"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11847212"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Yonat Tzur, Serafima Dubnov, Nimrod Madrer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ribosomal protein L24 mediates mammalian microRNA processing in an evolutionarily conserved manner."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Mol Life Sci (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00018-023-05088-w"}], "href": "https://doi.org/10.1007/s00018-023-05088-w"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38261097"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38261097"}]}]}]}