Abstract

Septins comprise a conserved family of proteins that are found primarily in fungi and animals. These GTP-binding proteins have several roles during cell division, cytoskeletal organization and membrane-remodelling events. One factor that is crucial for their functions is the ordered assembly of individual septins into oligomeric core complexes that, in turn, form higher-order structures such as filaments, rings and gauzes. The molecular details of these interactions and the mechanism by which septin-complex assembly is regulated have remained elusive. Recently, the first detailed structural views of the septin core have emerged, and these, along with studies of septin dynamics in vivo, have provided new insight into septin-complex assembly and septin function in vivo.

Author affiliations

1. Institute of Biochemistry, ETH Zürich, 8093 Zürich, Switzerland.
2. Institute of Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.

Correspondence to: Yves Barral¹ Email: yves.barral@bc.biol.ethz.ch

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