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Caspase recruitment domain family member 6 (CARD6) is a microtubule-associated regulatory protein containing a caspase recruitment domain (CARD), which is an antiparallel six-helix bundle that mediates homotypic protein–protein interactions[1][5]. CARD6 interacts with receptor-interacting protein kinases (RIP1 and RIP2/RICK/CARDIAK) and other CARD domain-containing proteins (including NOD1), playing a role in modulating signal transduction pathways converging on the nuclear factor kappa-B (NF-κB) transcription factor, a critical mediator of immune and inflammatory responses[1][2]. Through these interactions, CARD6 can positively or negatively regulate NF-κB activation in response to various innate immune signals and stressors[1][2]. CARD6 also associates with microtubules and may participate in spatial organization of signaling complexes, with a modulatory—not essential—role in apoptosis, inflammation, and likely innate immune pathway assembly[1][3][5]. There is no current evidence for direct pharmacological targeting of CARD6[5].
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