Discovering how pore forming proteins evolve different assembly and targeting mechanisms
Pore forming proteins are proteins that can literally punch holes (pores) into target cell membranes. There are over 30 different types of pore forming proteins that have evolved independently but one of the most fascinating is the MACPF/CDC superfamily. The MACPF/CDC proteins can oligomerise into a ring-shaped transmembrane beta-barrel pore capable of either direct cell lysis or the passive transport other large protein toxins. Members of the MACPF/CDC superfamily are found in all kingdoms of life with a range of functions including as immune effectors, pathogenicity factors, parasite egress, fungal defence and marine toxins. Whilst current structural biology research on the MACPF/CDC family suggest there is a common domain and a common pore structure for the family, there is a wide variation in the assembly pathways observed. Recent research using combinations of structure and single molecule imaging methods explains how and why different members have evolved different assembly pathways to suit their evolved function.
