{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nYWHAG – the gene encoding the 14‐3‐3γ isoform – acts as a pivotal adaptor in cell cycle regulation and signal transduction. Notably, 14‐3‐3γ modulates the subcellular distribution of key regulators by sequestering phosphorylated proteins such as p27 and by coordinating checkpoint responses. For example, its binding to phosphorylated Chk1 (at Ser296) and the formation of complexes with regulators such as KSR1, p21, and Plk1 enable proper mitotic progression and centrosome duplication while preventing premature cell cycle transitions. In these ways, YWHAG sustains genome integrity and calibrates mitotic fidelity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to these cell‐cycle functions, YWHAG critically influences cell fate in both normal development and disease. Its expression and activity are precisely tuned by several microRNAs and long noncoding RNAs that impinge on diverse signaling pathways. For instance, miR‐181b‐3p, miR‐509-5p, miR‐217, and miR‐30a-5p target YWHAG to modulate Snail stabilization, epithelial–mesenchymal transition and migration in breast cancer, non–small cell lung cancer and glioblastoma, while genetic deletions or de novo mutations affecting YWHAG contribute to neurodevelopmental disorders and epileptic encephalopathies. Moreover, altered YWHAG levels have been linked to aberrant adipocyte metabolism and poor clinical outcomes in several human cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "21"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, YWHAG engages its phosphorylated targets via highly specific binding modes that have been elucidated by structural and biophysical studies. Its interaction with substrates such as phosphorylated tyrosine hydroxylase, Hsp20, and the N-terminal motif of ANO1 not only determines their subcellular localization but also modulates their activity and membrane association. In addition, 14‐3‐3γ has been implicated in orchestrating intracellular trafficking events—such as the en bloc budding and fission of Golgi-derived carriers—and in regulating intercellular adhesion via desmosomal components. These diverse binding and structural properties underscore YWHAG’s central role as a versatile signal integrator."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "22", "end_ref": "34"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Toshihiro Sekimoto, Masahiro Fukumoto, Yoshihiro Yoneda "}, {"type": "b", "children": [{"type": "t", "text": "14-3-3 suppresses the nuclear localization of threonine 157-phosphorylated p27(Kip1)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.emboj.7600198"}], "href": "https://doi.org/10.1038/sj.emboj.7600198"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15057270"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15057270"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Lucas R Jagemann, Luís G Pérez-Rivas, E Josué Ruiz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The functional interaction of 14-3-3 proteins with the ERK1/2 scaffold KSR1 occurs in an isoform-specific manner."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M709185200"}], "href": "https://doi.org/10.1074/jbc.M709185200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18426801"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18426801"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Amol S Hosing, Samrat T Kundu, Sorab N Dalal "}, {"type": "b", "children": [{"type": "t", "text": "14-3-3 Gamma is required to enforce both the incomplete S phase and G2 DNA damage checkpoints."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Cycle (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4161/cc.7.20.6812"}], "href": "https://doi.org/10.4161/cc.7.20.6812"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18843201"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18843201"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Kousuke Kasahara, Hidemasa Goto, Masato Enomoto, et al. 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