{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPoly(A)‐specific ribibonuclease (PARN) is a key 3′ exoribonuclease that initiates mRNA decay by specifically removing poly(A) tails, thereby regulating mRNA stability and translation. Early biochemical purification and in vitro studies established its deadenylating activity during oocyte maturation and early embryogenesis, showing that PARN (initially termed DAN) is both nuclear and cytoplasmic and can be modulated by the m⁷G cap structure to enhance processivity. Mutagenesis and crystallographic analyses further revealed that a set of conserved acidic residues and multiple RNA‐binding domains (including an R3H domain and an RNA recognition motif) are essential for substrate recognition, catalysis, and dimer formation. In addition, interaction with ARE‐binding proteins such as TTP and CUG‐BP has been demonstrated to recruit or stimulate PARN activity, while studies in cancer cell models highlight its impact on cell proliferation through downstream effects on p53/p21 pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its canonical role in mRNA decay, PARN is critical for the biogenesis and maturation of several non‐coding RNAs central to telomere and ribosome homeostasis. By precisely trimming the 3′ ends of telomerase RNA (TERC), PARN ensures the production of functional, non‐oligoadenylated hTR; deficiency or mutation in PARN leads to the accumulation of aberrant, oligoadenylated precursors, which in turn causes telomere shortening and has been implicated in telomere syndromes such as familial pulmonary fibrosis and dyskeratosis congenita. PARN is also necessary for proper ribosomal RNA processing—as exemplified by its role in the final trimming steps of 18S rRNA maturation within pre-40S particles—thereby contributing to ribosome assembly and overall protein synthesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, PARN exerts finer control over post‐transcriptional gene regulation by modulating the 3′ end architecture of microRNAs and by dynamically interacting with nuclear proteins in response to cellular stress. For example, PARN trims excess nucleotides from microRNAs such as miR-122—thereby counterbalancing polyadenylation and ensuring proper miRNA maturation without substantially altering stability—and its activity is further influenced by binding partners including nucleolin, components of the cap-binding complex, and TOE1, as well as by stress-induced structural rearrangements in its C-terminal domain that alter its subcellular localization. These multifaceted regulatory roles exemplify how PARN integrates diverse signals to modulate the stability and processing of both coding and non-coding RNAs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "C G Körner, M Wormington, M Muckenthaler, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (1998)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/emboj/17.18.5427"}], "href": "https://doi.org/10.1093/emboj/17.18.5427"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "9736620"}], "href": "https://pubmed.ncbi.nlm.nih.gov/9736620"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "E Dehlin, M Wormington, C G Körner, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Interaction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitro."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2000)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s1097-2765(00)80442-6"}], "href": "https://doi.org/10.1016/s1097-2765(00"}, {"type": "t", "text": "80442-6) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "10882133"}], "href": "https://pubmed.ncbi.nlm.nih.gov/10882133"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "P R Copeland, M Wormington "}, {"type": "b", "children": [{"type": "t", "text": "The mechanism and regulation of deadenylation: identification and characterization of Xenopus PARN."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "RNA (2001)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1017/s1355838201010020"}], "href": "https://doi.org/10.1017/s1355838201010020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11424938"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11424938"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Yan-Guo Ren, Javier Martínez, Anders Virtanen "}, {"type": "b", "children": [{"type": "t", "text": "Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe(2+)-mediated cleavage."}]}, {"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.M111515200"}], "href": "https://doi.org/10.1074/jbc.M111515200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11742007"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11742007"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Wi S Lai, Elizabeth A Kennington, Perry J Blackshear "}, {"type": "b", "children": [{"type": "t", "text": "Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.23.11.3798-3812.2003"}], "href": "https://doi.org/10.1128/MCB.23.11.3798-3812.2003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12748283"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12748283"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Yan-Guo Ren, Leif A Kirsebom, Anders Virtanen "}, {"type": "b", "children": [{"type": "t", "text": "Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M403858200"}], "href": "https://doi.org/10.1074/jbc.M403858200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15358788"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15358788"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Mousheng Wu, Michael Reuter, Hauke Lilie, et al. 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