{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nBCL10 plays a central role as an adaptor protein in multiple receptor‐mediated signaling pathways that converge on the nuclear factor κB (NF‑κB) transcription factor. In lymphocytes, BCL10 is recruited into the CARMA–BCL10–MALT1 (CBM) complex following antigen receptor engagement—whether by the T‑cell receptor, B‑cell receptor, or even nonimmune receptors such as G protein–coupled receptors, epidermal growth factor receptor, Toll‑like receptor 4, and angiotensin II receptor—to promote NF‑κB activation. In these contexts, BCL10 functions as a molecular scaffold that, upon regulated post‐translational modification, facilitates the assembly of higher‑order signaling complexes through its polymerization (filament formation) and subsequent interactions with key effector molecules such as NEMO, MALT1, and various E3 ubiquitin ligases. This central role in propagating both canonical and noncanonical NF‑κB signals has been demonstrated in immune as well as nonimmune cells including endothelial, hepatic, and colonic epithelial cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular level, BCL10 function is tightly regulated by a series of post‑translational modifications that fine‑tune both the amplitude and duration of NF‑κB signaling. Phosphorylation events—mediated by kinases such as Rip2, Ca²⁺/calmodulin‑dependent kinase II, Akt1, and modulated by the phosphatase calcineurin—control BCL10’s oligomerization, its interaction with other CBM components, and even its nucleocytoplasmic distribution. In addition, BCL10 is subject to diverse ubiquitin modifications including lysine‑63–linked and linear ubiquitination (the latter mediated by ligases such as LUBAC), events required for bridging BCL10 to downstream effectors like the IκB kinase regulatory subunit NEMO. Other regulatory proteins—including the deubiquitylase A20, the COP9 signalosome subunit CSN5, and the E3 ligase MIB2—further impact the stability and signaling function of BCL10 by modulating its ubiquitination status. Collectively, these modifications ensure that BCL10-dependent NF‑κB activation occurs with appropriate intensity and duration."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical role in NF‑κB signaling, altered BCL10 activity and localization have been implicated in various disease settings and specialized cellular functions. Aberrant nuclear localization of BCL10 is a diagnostic marker in certain mucosa‑associated lymphoid tissue lymphomas and is associated with chromosomal translocations, while its dysregulated expression contributes to oncogenic processes in breast and B‑cell lymphomas. In addition, BCL10 has non‑canonical functions such as mediating cytoskeletal remodeling during phagocytosis in macrophages, and its deficiency or mutation can underlie combined immunodeficiency affecting both immune and nonimmune cells. These disease‐related aspects underscore the pathological consequences that arise when the formation or regulation of the CBM complex is disturbed."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "41"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Astrid A Ruefli-Brasse, Wyne P Lee, Stephen Hurst, et al. 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