Calpain-7 (CAPN7)

Calpain-7 (CAPN7) is a ubiquitously expressed, non-lysosomal, cysteine protease belonging to the calpain family of enzymes[1][2][3]. Structurally, calpains are typically heterodimers with large and small subunits, but Calpain-7 diverges from typical calpains and may function differently from classic calcium-dependent family members[2]. CAPN7 is recruited to the midbody during cell division by binding to the ESCRT-III subunit IST1 via its tandem MIT domains, a process required for efficient completion of cytokinetic abscission and for maintenance of the NoCut checkpoint—a surveillance pathway that delays the final separation of daughter cells in response to mitotic errors[1][3]. CAPN7 thus plays a crucial regulatory role in ensuring proper cell division, acting as a cofactor whose proteolytic activity is modulated by its interactions with ESCRT-III components. In addition to these roles in cytokinesis, CAPN7 is implicated in membrane trafficking processes and may have roles in endosomal sorting, cell migration, and invasion, as well as in reproductive biology where aberrant expression is associated with impaired embryo implantation[3][2]. Its direct physiological substrates in humans have not yet been identified, and no approved drugs are known to target CAPN7 specifically[1][2].

Other names

Calpain-7CAPN7PALBHPalBHpalB homologcalpain-like proteasehomolog of Aspergillus nidulans PALBCALPAIN7calpain-7calpain like proteasehomolog of Aspergillus Nidulans PALB