{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n ELP3 is the catalytic subunit of the highly conserved Elongator complex that exerts multifaceted functions in both the nucleus and the cytoplasm. In the nucleus, ELP3 contributes to transcriptional elongation by its histone acetyltransferase activity, thereby facilitating gene expression—for example, by promoting proper expression of stress‐responsive genes such as HSP70 through direct chromatin engagement (see."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": " In addition, structural studies have revealed that ELP3 binds transfer RNAs at the wobble position to facilitate chemical modifications that are essential for translation fidelity and proteome stability."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In the cytoplasm, ELP3 further extends its function beyond transcriptional regulation by acetylating non‐histone substrates. Notably, its acetylation of α‐tubulin is critical for proper neuronal maturation—affecting processes such as radial migration and branching of cortical projection neurons—and thus for the organization of the cytoskeleton."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}, {"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " ELP3 activity is also implicated in regulating the acetylation status of key metabolic and signaling enzymes; for instance, it functions as a potential acetyltransferase for glucose-6-phosphate dehydrogenase, thereby influencing the oxidative stress response"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": ", and it mediates the acetylation of PAK1, which in turn modulates hypoxia-induced autophagy relevant to glioblastoma progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Moreover, post-translational modification of ELP3 itself—for example, its phosphorylation on tyrosine residues by oncogenic kinases—adds an extra layer of regulation that may influence its enzymatic activities in tumor cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Interactions with transcription factors such as Sox2 further suggest that ELP3-mediated acetylation may also participate in controlling stem cell self-renewal and differentiation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " Collectively, these findings indicate that ELP3, through its dual role in modifying histones and non-histone proteins as well as tRNAs, plays a pivotal role in regulating gene expression, cytoskeletal dynamics, metabolic homeostasis, and cellular differentiation. Dysregulation of these processes has been linked to neurodevelopmental disorders and various cancers, positioning ELP3 as a promising target for therapeutic intervention.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Catherine Creppe, Lina Malinouskaya, Marie-Laure Volvert, et al. 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