Liprin-α and ELKS are two of the core constituents at the active zone, and have been studied genetically and electrophysiologically in both invertebrate and vertebrate systems. Despite a variety of interactions found between them and with other presynaptic proteins, there has been little information known about their biochemical performances and their roles in assembly, maintenance and function of active zone.

Here, we tried to characterize the two important presynaptic proteins, liprin-α and ELKS, through combination of different biochemical approaches. To further understand the molecular mechanism underlying their physiological roles at the active zone, we used purified recombinant proteins to verify those reported interactions in a more quantitative and conclusive biochemica...[ Read more ]

Liprin-α and ELKS are two of the core constituents at the active zone, and have been studied genetically and electrophysiologically in both invertebrate and vertebrate systems. Despite a variety of interactions found between them and with other presynaptic proteins, there has been little information known about their biochemical performances and their roles in assembly, maintenance and function of active zone.

Here, we tried to characterize the two important presynaptic proteins, liprin-α and ELKS, through combination of different biochemical approaches. To further understand the molecular mechanism underlying their physiological roles at the active zone, we used purified recombinant proteins to verify those reported interactions in a more quantitative and conclusive biochemical way. My results indicate the presence of a large protein complex mediated by multivalent bindings among these two proteins and their binding partners, which implicates their roles as active zone scaffolding proteins responsible for active zone assembly. In addition, their binding partners include cell adhesion molecules on the presynaptic membrane which may link these scaffolding proteins to the opposite postsynaptic terminal.