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Topic: α2δ-2

ePoster
3 ePosters

In Neuroscience

ePoster · Neuroscience

A biallelic mutation in CACNA2D2 associated with epileptic encephalopathy affects calcium channel-dependent as well as synaptic functions of α2δ-2

Sabrin Haddad, Cornelia Ablinger, Ruslan Stanika, Manuel Hessenberger, Marta Campiglio, Nadine J. Ortner, Petronel Tuluc, Gerald J. Obermair · FENS Forum 2024

The roles of auxiliary α2δ subunits of voltage-gated calcium channels (CaVs) in modulating channel membrane expression and calcium current properties are widely recognized. In addition, recent literature suggests an important role of α2δ proteins in synapse formation, differentiation, and synaptic wiring. Therefore, it is not surprising that α2δ proteins have been linked to neurological, neurodevelopmental, and neuropsychiatric disorders. Genetic variants of the α2δ-2 isoform have been associated with epileptic encephalopathy and cerebellar atrophy. In this study we performed a detailed functi

ePoster · Neuroscience

Elucidating the role of α2δ proteins in synapse organization

Clarissa Eibl, Ruslan Stanika, Cornelia Ablinger, Sabrin Haddad, Gerald J. Obermair · FENS Forum 2024

Neurons communicate via synapses to allow normal brain functions such as cognition, memory formation, and learning. In these processes, synapses show plasticity and can be remodeled. Synapse formation is driven by synapse-organizing proteins that span the synaptic cleft to orchestrate the alignment of pre- and postsynaptic molecules. Recently, presynaptic α2δ proteins have been identified as crucial organizers of synapses by regulating axonal wiring, presynaptic differentiation, and postsynaptic receptor clustering. So far, α2δ proteins have been extensively studied as subunits of the voltage-

ePoster · Neuroscience

Improved neuronal surface detection of α2δ proteins by nanobody immunolabeling

Ruslan Stanika, Manuel Hessenberger, Gerald J. Obermair · FENS Forum 2024

α2δ proteins serve as auxiliary subunits of voltage-gated calcium channels (CaV) and regulate the formation and differentiation of synapses. To comparatively study the neuronal localization of the four α2δ isoforms (α2δ-1 to -4), we previously established hemagglutinin (HA) tagging, which allows the surface detection with anti-HA antibody labeling. However, localizing α2δ proteins in synaptic membranes is limited because the synaptic cleft is densely packed with trans-synaptic and extracellular matrix proteins. Thus, classical antibodies have restricted access to extracellular epitopes. Here,