Septin 7 is a highly conserved GTP-binding filamentous protein. Septins are important for the organization of the actin cytoskeleton. Septin7 also plays an important role in cytokinesis, and membrane dynamics^1,2.

Septins were first discovered in yeast and since, 13 septin genes have been identified in mammals (SEPT1 to SEPT12 and SEPT14). The 13 gene-encoded proteins can be classified into four distinct subgroups based on their sequence homology of their domain structure².

Septins share a highly conserved structure composed of the central GTPase domain and N- and C-terminal domains of various lengths³. They self-assemble into higher-order structures, including filaments and rings in tri-, hexa-, or octameric complexes consisting of multiple septin polypeptides, which are typical for different cell types. The various septin isoforms seem to determine the function and regulation of the septin complex⁴.

Septin-7 regulates Ca²⁺ entry through Orai1 by regulating the opening of the channel⁵.

Dysregulation of septins leads to human diseases such as neurodegenerative and bleeding disorders. In non-dividing cells such as neuronal tissue and platelets septins have been associated with exocytosis^1,2.