{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe study described in the abstract (PMID"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "dissects a mechanism by which oxidative stress regulates peroxisomal protein import. In response to H₂O₂ exposure, the central peroxisomal membrane component Pex14 is phosphorylated at a specific serine residue (Ser232). This modification impairs the interaction between Pex14 (together with its receptor Pex5) and catalase—the hydrogen peroxide–decomposing enzyme—resulting in the selective inhibition of catalase import into peroxisomes and a consequent shift of catalase localization to the cytosol. This redistribution is proposed to bolster cellular resistance to oxidative stress. Although the query asks for a summary of the function of MIR6846, the abstract does not mention or describe any role for MIR6846. Thus, based on the provided abstract, no function or regulatory involvement of MIR6846 can be identified within this context.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kanji Okumoto, Mahmoud El Shermely, Masanao Natsui, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The peroxisome counteracts oxidative stresses by suppressing catalase import via Pex14 phosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Elife (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7554/eLife.55896"}], "href": "https://doi.org/10.7554/eLife.55896"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32831175"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32831175"}]}]}]}