Abstract
Purpose: Septins in eukaryotes belong to a strongly conserved group of proteins, the members of which are increasingly noted as ‘the fourth component’ of the cytoskeleton. All septin types have a GTP binding domain, form heterohexamer complexes that can arrange into higher order structures, such as filaments and rings. Septins are also known to form cell membrane domains in the proximity of endoplasmic reticulum punctae, which are believed to play a key role during STIM1-Orai1 coupling during store-operated calcium entry (SOCE).
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