Topic: protein-protein interactions

Animals exhibit a stunning array of natural behaviors, many of which are innate and controlled by intricate neural circuits genetically specified. In the fruit fly, connectomics work has revealed precise patterns of neuronal connectivity and their computational potential. However, we lack a molecular understanding of how such circuit connectivity is established with synaptic specificity, in part because it remains challenging to define the molecular landscape and interactions at subcellular resolution in intact tissue. Taking advantage of the well-defined and accessible Drosophila motion visio

GABAA receptors (γ-aminobutyric acid-gated receptors type A) are the essential structural and functional postsynaptic components of inhibitory synapses in the mammalian brain. They belong to a family of GABA-gated Cl/HCO3-permeable ion channels which are built as hetero-pentamers of subunits classified as α(1-6), β(1-3), γ(1-3), δ, ε, π, θ and ρ(1-3). How, where, and when the inhibitory synapses are formed is tightly regulated during early brain development and later synaptogenesis by genetic and environmental factors. Multiple proteins have been shown to participate in the initiation and func

The application of biotin ligase or peroxidase fused with specific proteins or subcellular regions, combined with mass spectrometry-based quantitative proteomics, has become a potent approach for unravelling molecular interactions and determining the locations of native proteins based on their proximity. Recent applications of proximity-dependent biotinylation in neuroscience have yielded insights into the composition of sub-synaptic structures, including the synaptic cleft [1].Despite the effectiveness of proximity labelling methods in providing a global perspective on protein-protein interac