{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMALT1 is a central mediator of antigen receptor and cytokine receptor signaling, functioning primarily as a scaffold that organizes the formation of CBM (CARMA–BCL10–MALT1) signalosomes to activate the canonical NF‑κB pathway. In endothelial and immune cells, signals from stimuli such as CXCL8/IL8, T‑cell receptor engagement, or other receptors induce the assembly of complexes that link upstream events to IκB kinase activation and subsequent NF‑κB–dependent gene expression, thereby regulating processes as diverse as VEGF autocrine stimulation, interleukin production, and adaptive immune responses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its adaptor role, MALT1 functions as an active paracaspase whose proteolytic activity refines and amplifies NF‑κB signaling. Upon immune stimulation, MALT1 cleaves several negative regulators and specific NF‑κB family members—including substrates such as A20, CYLD, and RelB—thereby facilitating rapid and sustained transcriptional responses. This protease activity is tightly regulated by posttranslational modifications such as monoubiquitination at key lysine residues and by dimerization, while alternative splicing further modulates its ability to recruit downstream effectors. Moreover, small-molecule inhibitors (such as MI‑2 and phenothiazine derivatives) directly target MALT1’s catalytic activity, underscoring its druggability."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of MALT1 signaling is implicated in various pathologic conditions. Constitutive MALT1 activity—often driven by chromosomal translocations (e.g. API2‑MALT1 fusions), promoter deregulation, and splice variant imbalances—promotes survival and proliferation in activated B‑cell lymphomas and MALT lymphomas, while also contributing to immune disorders such as psoriasis and impacting other malignancies (for example, EGFR‑driven breast cancers). Studies have demonstrated that interfering with MALT1 protease function not only impairs aberrant NF‑κB activation and cytokine production but may also reverse disease phenotypes, positioning MALT1 as an attractive therapeutic target in cancer, autoimmunity, metabolic dysregulation, and even in control of latent viral reservoirs."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Daniel Martin, Rebeca Galisteo, J Silvio Gutkind "}, {"type": "b", "children": [{"type": "t", "text": "CXCL8/IL8 stimulates vascular endothelial growth factor (VEGF) expression and the autocrine activation of VEGFR2 in endothelial cells by activating NFkappaB through the CBM (Carma3/Bcl10/Malt1) complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.C800207200"}], "href": "https://doi.org/10.1074/jbc.C800207200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19112107"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19112107"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Michael Düwel, Verena Welteke, Andrea Oeckinghaus, et al. 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