{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nBeta‐actin (ACTB) is a ubiquitously expressed cytoskeletal protein that underpins cellular architecture, motility, and developmental programs. Numerous studies have shown that mutations or altered expression of ACTB disrupt normal cell shape and migration, leading to a spectrum of developmental disorders, including Baraitser–Winter syndrome, as well as neurological defects such as dystonia and sensory impairments. In several soft tissue tumors, ACTB participates in oncogenic gene‐fusion events (for example, ACTB–GLI1 and ACTB–FOSB), whereby its constitutively active promoter drives deregulated expression of fusion partners that contribute to tumorigenesis and metastatic behavior. Moreover, gain‐of‐function mutations in ACTB have been linked to aberrant cytoskeletal dynamics and neutrophil dysfunction in cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its classical role in maintaining cytoplasmic structure, beta‐actin plays critical roles within the nucleus. It participates in transcriptional regulation by associating with RNA polymerases and transcription complexes—including those involved in RNA polymerase III–mediated U6 snRNA transcription—as well as by contributing to chromatin remodeling and the assembly of elongating complexes. Beta‐actin folding by chaperonin complexes (e.g., CCT) and post‐translational modifications such as SETD3‐mediated methylation and nitric oxide–dependent S-nitrosylation further modulate its function, while its mRNA stability is controlled by factors such as HuR. Collectively, these processes influence cell proliferation, differentiation, and immune responses while also affecting cell–cell adhesion and polarity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in transcription and basal cellular architecture, beta‐actin is dynamically regulated during processes such as cell adhesion, stress response, and immune synapse formation. Its interactions with a range of binding partners—including protein disulfide isomerase, MARCKS, chorein, and AIM1—as well as with viral proteins (for example, the measles virus matrix protein) underscore its involvement in regulating actin polymerization, filament organization, and signal transduction pathways underlying apoptosis, cytoskeletal remodeling, and metastatic progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Anna Dahlén, Christopher D M Fletcher, Fredrik Mertens, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "A mutation of beta -actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystonia."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1086/504271"}], "href": "https://doi.org/10.1086/504271"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16685646"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16685646"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Jean-Baptiste Rivière, Bregje W M van Bon, Alexander Hoischen, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Severe forms of Baraitser-Winter syndrome are caused by ACTB mutations rather than ACTG1 mutations."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Hum Genet (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ejhg.2013.130"}], "href": "https://doi.org/10.1038/ejhg.2013.130"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23756437"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23756437"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Nikolas Hundt, Matthias Preller, Olga Swolski, et al. 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