Topic: dSTORM

Pathological protein aggregation and synaptic dysfunction are major contributors to neurodegenerative disorders. However, understanding disease-relevant protein aggregation, such as Beta-amyloid, Alpha-synuclein and Tau aggregation within synapses, remains limited. To address this, we present a novel method for visualizing protein aggregates in individual synaptosomes. We combined Single-molecule Pull Down (SiMPull) and direct Stochastic Optical Reconstruction Microscopy (dSTORM), to immobilize individual synaptosomes and characterize single aggregates within them with ~20nm spatial resolution

Synapses are established and maintained by adhesion molecules, which include post-synaptic neuroligins (NLGNs). In the absence of highly specific antibodies, the sub-cellular distribution and synaptic function of NLGNs have been extensively manipulated using knock-out, over-expression or rescues approaches, leading to controversial results. In this context, we generated a new transgenic knock-in mouse strain in which endogenous NLGN1 has been N-terminally tagged with a biotin acceptor peptide (bAP) by gene editing using the CRISPR-Cas-9 strategy. Native NLGN1 can be enzymatically biotinylated