Protein tyrosine phosphatase non-receptor type 23 (PTPN23)

Protein tyrosine phosphatase non-receptor type 23 (PTPN23) is a cytosolic enzyme belonging to the PTP superfamily, which regulates the phosphorylation state of proteins on tyrosine residues. PTPN23 plays key roles in endosomal sorting via the ESCRT complex, acts as a tumor suppressor, and is involved in pre-mRNA splicing, ciliogenesis, and maintenance of cardiac T-tubule organization. It interacts with sarcomeric and membrane-associated proteins (e.g., α-actinin, dystrophin-glycoprotein complex) and participates in cytoskeletal anchoring in cardiomyocytes. Dysregulation of PTPN23 has been linked to neurodevelopmental disorders, structural brain anomalies, various cancers, and cardiac dysfunction. As with other protein tyrosine phosphatases, targeting PTPN23 for therapeutic modulation poses significant challenges due to the highly conserved nature of PTP active sites and potential for widespread effects on cellular signaling networks[1][2][4][5].

Other names

HD-PTPKIAA1471PTP-TD14DKFZP564F0923His domain-containing protein tyrosine phosphataseProtein tyrosine phosphatase TD14HDPTPNEDBASS

Inhibitors would block its phosphatase activity, potentially restoring or modulating signal transduction related to tumorigenesis, cellular differentiation, or other signaling pathways