A biochemical view on the septins, a less known component of the cytoskeleton.

Abstract

The septins are a conserved family of guanine nucleotide binding proteins, often named the fourth component of the cytoskeleton. They self-assemble into non-polar filaments and further into higher ordered structures. Properly assembled septin structures are required for a wide range of indispensable intracellular processes such as cytokinesis, vesicular transport, polarity establishment and cellular adhesion. Septins belong structurally to the P-Loop NTPases. However, unlike the small GTPases like Ras, septins do not mediate signals to effectors through GTP binding and hydrolysis. The role of nucleotide binding and subsequent GTP hydrolysis by the septins is rather controversially debated. We compile here the structural features from the existing septin crystal- and cryo-EM structures regarding protofilament formation, inter-subunit interface architecture and nucleotide binding and hydrolysis. These findings are supplemented with a summary of available biochemical studies providing information regarding nucleotide binding and hydrolysis of fungal and mammalian septins.