Adenylyl cyclase-associated protein 1 (CAP1)

Adenylyl cyclase-associated protein 1 (CAP1) is a highly conserved, multifunctional protein that plays a critical role in regulating the actin cytoskeleton and cellular signaling pathways (UniProt Q01518). It primarily functions by accelerating the turnover of actin filaments through its interaction with cofilin and actin monomers, thereby facilitating cell migration, endocytosis, and morphogenesis (NCBI Gene ID: 10487). Beyond its structural roles, CAP1 serves as a key signaling transducer, notably acting as a functional receptor for human resistin, which links it to inflammatory responses and metabolic disorders like obesity and type 2 diabetes (Lee et al., 2014, Cell Metabolism). In oncology, CAP1 is frequently overexpressed and is associated with increased cell proliferation, epithelial-mesenchymal transition (EMT), and metastasis in various cancers, including breast, lung, and pancreatic malignancies (Zhang et al., 2019, Journal of Experimental & Clinical Cancer Research). While there are currently no FDA-approved drugs targeting CAP1, it is an area of active research for the development of novel therapeutics aimed at disrupting its interaction with resistin or its role in tumor progression. The protein's involvement in both metabolic and oncogenic pathways makes it a versatile target for multi-disease therapeutic strategies, although its ubiquitous expression presents a challenge for achieving tissue-specific inhibition.

Other names

CAP1CAPAdenylate cyclase-associated protein 1

CAP1 regulates actin filament dynamics by promoting cofilin-mediated severing and recycling of actin monomers; it also acts as a cell surface receptor for resistin to activate cAMP-PKA-NF-kB signaling pathways (Lee et al., 2014; UniProt Q01518).