Structural studies of the C-terminal tail of polycystin-2 (PC2) reveal insights into the mechanisms used for the functional regulation of PC2

摘要: Mutations in polycystin-2 (PC2) lead to autosomal dominant polycystic kidney disease (ADPKD). The molecular mechanism linking mutations PC2 and the pathogenesis of ADPKD is not well understood. Therefore, understanding functional regulation its interaction with other proteins under both physiological pathogenic conditions important for elucidating identifying potential targets treatment. Normally, functions as a calcium-permeable channel whose activity regulated by calcium binding C-terminal domain (PC2 Cterm). Cterm also involved assembly hetero-oligomerization partners cells. Different domains have been studied using structural approaches. Within Cterm, there calcium-binding EF-hand domain, crucial calcium-dependent channel. Downstream lies coiled-coil region, which hetero-interaction protein. can form an oligomer, mediated region. Although has extensively relationship importance regulation, are misunderstandings respect definition topology within role each domain. Here, we review previous studies that connect properties distinct aspects regulation.