Neuronal-specific septin-3 (SEPT3)

Neuronal-specific septin-3 (SEPTIN3) is a member of the septin family of filament-forming GTP-binding proteins[3][2][1]. SEPTIN3 is highly expressed in neurons, especially in brain tissue, and is thought to play roles in synaptic vesicle recycling and maintenance of membrane compartmentalization, possibly by forming diffusion barriers and scaffolds for protein assembly at intracellular sites[1]. Structurally, SEPTIN3 can assemble into filaments and heterooligomeric complexes—most notably with SEPT5 and SEPT7 in rat brain[1]. It contains a GTP-binding domain (G-domain), is capable of nucleotide binding, and forms unique interfaces critical for filament assembly[2][4]. SEPTIN3-group members distinguish themselves by lack of a C-terminal coiled-coil domain, a structural element present in other septins[4]. The biological function of SEPTIN3 is not fully elucidated, and while septins as a group are linked to diverse cellular mechanics, SEPTIN3 itself is not associated with direct drug targeting, disease mutation, or clinical biomarker status[3][1].

Other names

Neuronal-specific septin-3SEPTIN3SEP3SEPT3bK250D10.3

Not applicable (no approved drugs or well-characterized experimental modulators for SEPTIN3)