{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nYWHAQ, which encodes a 14‐3‐3 isoform, exemplifies the role of 14‐3‐3 adaptor proteins in transducing phosphorylation‐dependent signals. In multiple contexts, 14‐3‐3 proteins bind phosphorylated targets to modulate their subcellular localization and activity. For example, phosphorylation of the Yes‐associated protein (YAP) by Akt promotes its binding to 14‐3‐3, sequestering YAP in the cytoplasm and thereby attenuating its pro‐apoptotic transcriptional coactivator function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Similarly, Akt‐dependent phosphorylation of p27 at Thr198 enables its cytoplasmic retention via 14‐3‐3 binding, which in turn facilitates cell cycle progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Moreover, autoantibody profiling in lung cancer has identified 14‐3‐3 proteins as immunogenic targets, underscoring their potential as biomarkers"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": ", while in neurons phosphorylation of SRPK2 enhances its binding to 14‐3‐3 to restrict cell cycle reentry and apoptosis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " In addition, detection of autoantibodies against 14‐3‐3 theta in lung cancer sera"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "and the regulatory role of 14‐3‐3 tau in mediating p21 degradation to promote the G1/S transition"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "further emphasize the central role of 14‐3‐3 isoforms in cell survival and proliferation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond their role in signal transduction and cell cycle control, 14‐3‐3 proteins are crucial regulators of intracellular trafficking and assembly of multiprotein complexes. Phosphorylated AS160, upon stimulation by insulin or growth factors, binds 14‐3‐3 proteins to facilitate GLUT4 translocation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": ", while phosphorylation of β2 integrin switches binding from filamin to 14‐3‐3, thereby modulating T‐cell adhesion."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " During cytokinesis, phosphorylation of centralspindlin components regulates their clustering through reversible association with 14‐3‐3"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": ", and 14‐3‐3 proteins also serve as diagnostic markers in neurodegenerative conditions such as Creutzfeldt–Jakob disease."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " Similarly, sequestration of transcription factors such as FOXO3a by 14‐3‐3 restricts their nuclear import"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "and C‐RAF’s subcellular localization is likewise regulated by 14‐3‐3 binding."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": " The interaction between Sirt2 and specific 14‐3‐3 isoforms modulates p53 deacetylation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": ", and phosphorylation of NoxA1 promotes its binding to 14‐3‐3, thereby regulating reactive oxygen species production."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": " Reviews and studies further outline how 14‐3‐3 proteins not only form dimers and even function as monomers in certain regulatory contexts"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}, {"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": ", but also control nuclear import of HDAC4"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": ", impose steric inhibition on FOXO4’s DNA binding"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": ", and regulate serotonin biosynthesis via tryptophan hydroxylase."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " In the nervous system, formation of complexes with Hsp60 and the cellular prion protein further illustrate diverse chaperone‐like functions"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": ", while studies in platelets reveal that 14‐3‐3 association with membrane proteins influences adhesion"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": "and sorting regulators such as hMex‑3B."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn various disease settings, 14‐3‐3 proteins—including the isoform encoded by YWHAQ—emerge as pivotal modulators of pathological signaling. Their interaction with transcription factors such as ETV1 stabilizes oncogenic programs in prostate cancer"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": ", and binding to the follicle-stimulating hormone receptor modulates downstream signaling in reproductive tissues."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": " In response to DNA damage, phosphorylation cascades involving Lats2 initiate modifications of 14‐3‐3 proteins that are critical for P-body assembly"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": ", while regulation of ASK kinase signaling is also mediated through dual engagement with 14‐3‐3."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": " Studies in diabetic cardiomyopathy demonstrate that impaired 14‐3‐3 function exacerbates pathological cardiac remodeling"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "27"}]}, {"type": "t", "text": ", and modulation of 14‐3‐3 interactions by small molecules such as fusicoccin influences platelet function"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "28"}]}, {"type": "t", "text": "as well as von Willebrand factor-mediated adhesion."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "29"}]}, {"type": "t", "text": " Moreover, inhibition of RGS proteins by 14‐3‐3 alters G protein signaling"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "30"}]}, {"type": "t", "text": ", and their presence within extracellular vesicles points to roles in intercellular communication."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "31"}]}, {"type": "t", "text": " Additional diagnostic applications include using CSF 14‐3‐3 detection as a surrogate marker in neurological disorders such as Guillain–Barré syndrome."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "32"}]}, {"type": "t", "text": " Finally, in metabolic regulation, 14‐3‐3 binding impacts mTORC1 signaling through PRAS40"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "33"}]}, {"type": "t", "text": "and interacts with PITP proteins to modulate lipid transfer"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "34"}]}, {"type": "t", "text": ", while emerging biomarker studies link 14‐3‐3 alterations with chemotherapy resistance."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Subham Basu, Nicholas F Totty, Meredith S Irwin, et al. 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