Caspase recruitment domain-containing protein 10 (CARD10) (CARD10)

Caspase recruitment domain-containing protein 10 (CARD10), also known as CARMA3, is a scaffold protein that plays a critical role in linking G protein-coupled receptors (GPCRs) to the NF-kappaB signaling pathway [1, 2]. It belongs to the membrane-associated guanylate kinase (MAGUK) family and is characterized by its N-terminal CARD domain, which facilitates protein-protein interactions [1]. CARD10 forms the CBM complex alongside BCL10 and MALT1, which is essential for transmitting signals from various stimuli, including lysophosphatidic acid (LPA) and angiotensin II, to activate the IKK complex [3, 4]. This activation leads to the nuclear translocation of NF-kappaB, promoting cell survival, proliferation, and inflammatory responses [4]. In many cancers, such as lung and breast cancer, CARD10 is frequently overexpressed, driving tumor progression and resistance to apoptosis [3, 5]. Consequently, it is considered a promising therapeutic target for oncology and chronic inflammatory conditions [5]. While specific clinical inhibitors for CARD10 are still in development, targeting the CBM complex components remains a significant area of pharmacological research [4].

Other names

CARMA3BIMP1Caspase recruitment domain family member 10Bcl10-interacting MAGUK protein 1

Acts as a scaffold to assemble the CARD10-BCL10-MALT1 (CBM) complex, which bridges G protein-coupled receptors (GPCRs) to the IKK complex, leading to NF-kappaB activation [3, 4].