CARD9
CARD9
CARD9, also known as caspase recruitment domain-containing protein 9, is a crucial protein involved in the regulation of immune responses. It plays a significant role in various cellular processes, particularly in the activation of innate immune signaling pathways.
Structure[edit | edit source]
CARD9 is a member of the caspase recruitment domain (CARD)-containing protein family. It consists of several domains, including an N-terminal CARD domain, a coiled-coil domain, and a C-terminal domain. These domains enable CARD9 to interact with other proteins and participate in signal transduction pathways.
Function[edit | edit source]
CARD9 functions as an adaptor protein in the innate immune system. Upon activation of pattern recognition receptors (PRRs) by microbial components, such as pathogen-associated molecular patterns (PAMPs), CARD9 is recruited to the signaling complex. It then mediates the activation of downstream signaling cascades, leading to the production of pro-inflammatory cytokines and antimicrobial responses.
Role in Disease[edit | edit source]
Mutations in the CARD9 gene have been associated with various inflammatory disorders, including inflammatory bowel disease (IBD), fungal infections, and autoimmune diseases. Dysregulation of CARD9 signaling can lead to aberrant immune responses and increased susceptibility to infections.
Interactions[edit | edit source]
CARD9 interacts with multiple proteins involved in immune signaling pathways, such as NF-κB and MAPK signaling molecules. These interactions are essential for the proper activation of immune responses and the maintenance of immune homeostasis.
Clinical Significance[edit | edit source]
Understanding the role of CARD9 in immune regulation has implications for the development of therapeutic strategies targeting immune-related diseases. Targeting CARD9 signaling pathways may offer new opportunities for the treatment of inflammatory conditions and infectious diseases.
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Contributors: Prab R. Tumpati, MD