Presentation description

Calpain-7 (CAPN7), a member of the calpains family, is a calcium-dependent cysteine protease expressed in mammalian cells. Previous studies identified CAPN7 as a cofactor in the ESCRT-III pathway, a critical mediator of the membrane fission step, in which CAPN7 is recruited to the midbody by the ESCRT-III protein IST1, where it is essential towards efficient abscission and NoCut checkpoint maintenance. However, while binding partners of CAPN7 have been identified, its proteolytic substrate(s) remain unknown. In this project, we sought to determine the novel substrates of CAPN7 by individually expressing its component subunits. To identify potential binding partners, the CAPN7 subunits were cloned in pLVX vectors along with a TurboID-GFP construct, which allowed for identification of candidate substrates through the use of enzyme-catalyzed proximity-labeling. We successfully isolated clones for the CAPN7 domains, with future studies seeking to express the relevant proteins and determine potential binding partners of each component subunit.