Adenylyl cyclase-associated protein 1 (CAP1) (CAP1)

Adenylyl cyclase-associated protein 1 (CAP1) is a multifunctional protein that serves as a critical regulator of actin cytoskeleton dynamics and a cell-surface receptor for the pro-inflammatory cytokine resistin (Lee et al., 2014, Cell Metabolism). In humans, CAP1 is expressed on the surface of monocytic immune cells, including the THP-1 cell line, where it mediates the inflammatory effects of resistin (UniProt Q01518). Binding of resistin to the SH3-binding domain of CAP1 triggers an increase in intracellular cyclic AMP (cAMP) levels, subsequently activating protein kinase A (PKA) and the NF-κB signaling pathway (Jang et al., 2023, Int. J. Mol. Sci.). This cascade promotes the transcription of various pro-inflammatory cytokines, contributing to the pathogenesis of chronic inflammatory conditions such as atherosclerosis, type 2 diabetes, and obesity-related insulin resistance. Additionally, CAP1's role in actin filament turnover makes it a key player in cell migration and morphology. Therapeutic interest in CAP1 focuses on disrupting the resistin-CAP1 interaction to mitigate chronic inflammation and its associated metabolic complications.

Other names

Cyclase-associated protein 1CAP1Adenylate cyclase-associated protein 1CAP, adenylate cyclase-associated protein, 1

Resistin binds to the SH3-binding domain of CAP1 on the surface of monocytes, which increases intracellular cAMP levels and activates the PKA and NF-κB signaling pathways to induce pro-inflammatory cytokine expression.