{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nZFP36 (also known as tristetraprolin or TTP) is a key RNA‐binding protein that recognizes AU‐rich elements (AREs) in the 3′ untranslated regions of many labile mRNAs and promotes their rapid decay. Through its tandem zinc‐finger domain, ZFP36 binds specific sequence motifs within targets such as tumor necrosis factor–α, granulocyte–macrophage colony–stimulating factor, vascular endothelial growth factor, programmed death ligand–1, and other cytokine and inflammation‐associated transcripts. By recruiting components of the mRNA decay machinery—including deadenylases (for example, those in the CCR4-NOT complex and PARN) and decapping enzymes—it accelerates deadenylation and decapping, thereby ensuring tight posttranscriptional control of gene expression. This RNA binding and decay-promoting function has been characterized by biochemical, structural, and cell-free assays that reveal a dynamic peptide–RNA interaction and conformational changes important for high-affinity recognition of AREs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe activity of ZFP36 is exquisitely regulated by posttranslational modifications and subcellular localization. Key signaling pathways—including those mediated by p38 MAPK, MK2, ERK, and other kinases—phosphorylate ZFP36, which in many cases inhibits its ability to recruit the decay machinery by, for example, promoting sequestration in complexes with 14-3-3 proteins. Moreover, ZFP36 can shuttle between the nucleus and the cytoplasm and is rapidly redistributed to stress granules and processing bodies, where it can nucleate the assembly of mRNP complexes and thereby modulate mRNA translation and decay. Feedback mechanisms also exist whereby ZFP36 binds to its own mRNA to autoregulate its expression, maintaining a balance in the cellular response to inflammatory stimuli."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn various pathological contexts—including chronic inflammation and cancer—dysregulation or diminished expression of ZFP36 results in the aberrant stabilization of proinflammatory, proliferative, and pro-angiogenic mRNAs. In several tumor models, low levels or impaired function of ZFP36 have been linked to increased expression of cytokines, chemokines, matrix metalloproteinases, and other factors that promote tumor cell invasion and metastasis. Moreover, cross-regulatory circuits involving antagonistic RNA-binding proteins (for example, HuR) and microRNAs further modulate ZFP36 expression and activity, highlighting its importance as a molecular rheostat that can restrict cancer progression and temper inflammatory responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "P J Blackshear "}, {"type": "b", "children": [{"type": "t", "text": "Tristetraprolin and other CCCH tandem zinc-finger proteins in the regulation of mRNA turnover."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Soc Trans (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/bst0300945"}], "href": "https://doi.org/10.1042/bst0300945"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12440952"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12440952"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Perry J Blackshear, Wi S Lai, Elizabeth A Kennington, et al. 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