Subcellular localisation of recombinant Densin-180 clones expressed in HEK293 TSA cells

Densin-180 is one of the first discovered, most abundant and, yet, most obscure core components of the postsynaptic density, a specialised structure playing a key role in synaptic transmission of excitatory neurons in the central nervous system, a process fundamental to the learning and memory processes of the brain. A founding member of the LAP (Leucine-rich repeat and PDZ domain containing) protein family, it features 16 leucine-rich repeat domains, 2 LAP specific domains, a phosphorylation rich region and a PDZ domain, and has identified interactions with a number of PSD components which include CaMKII-α, α-actinin, Cav1.3 (L-type Ca2+) channels, MAGUIN-1, δ-catenin and Shank. Densin-180 is thought to function as a key adapter protein, coordinating cytoskeletal, scaffolding and receptor molecules in the adaptation, maintenance and regulation of the highly dynamic cell to cell contacts that are synapses of the CNS. Here, we present 9 eGFP-tagged Densin-180 fusion constructs for the detailed study of Densin-180’s function and show that C-terminal PDZ domain and C-terminal terminal amino acid mediated protein-protein interactions play a key role in Densin-180 punctate behaviour in HEK 293 TSA Cells