The Physiological Function of nNOS-Associated CAPON Proteins and the Roles of CAPON in Diseases

In this review, the structure, isoform, and physiological role of the carboxy-terminal PDZ ligand of neuronal nitric oxide synthase (CAPON) are summarized. There are three isoforms of CAPON in humans, including long CAPON protein (CAPON-L), short CAPON protein (CAPON-S), and CAPON-S' protein. CAPON-L includes three functional regions: a C-terminal PDZ-binding motif, carboxypeptidase (CPE)-binding region, and N-terminal phosphotyrosine (PTB) structural domain. Both CAPON-S and CAPON-S' only contain the C-terminal PDZ-binding motif. The C-terminal PDZ-binding motif of CAPON can bind with neuronal nitric oxide synthase (nNOS) and participates in regulating NO production and neuronal development. An overview is given on the relationship between CAPON and heart diseases, diabetes, psychiatric disorders, and tumors. This review will clarify future research directions on the signal pathways related to CAPON, which will be helpful for studying the regulatory mechanism of CAPON. CAPON may be used as a drug target, which will provide new ideas and solutions for treating human diseases.

Automated summary

This review summarizes the structure, isoforms, and physiological role of CAPON, as well as its relationship with heart diseases, diabetes, psychiatric disorders, and tumors. The C-terminal PDZ-binding motif of CAPON plays a regulatory role in nitric oxide production and neuronal development. Clarifying the future research directions on the signal pathways related to CAPON will facilitate the study of its regulatory mechanism and provide new ideas for treating human diseases.