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. 2017 Feb 7;5:3. doi: 10.3389/fcell.2017.00003

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Copyright © 2017 Neubauer and Zieger.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) Schematic septin domain structure. Septins share a conserved GTP-binding domain, a phosphoinosite-binding polybasic region (PBR), a septin unique domain (SUD), and most of them one or more coiled-coil domains. The length and amino acid sequence of the N- and C-terminus vary (according to Trimble, 1999). (B) Homology-based subgroups. The 13 human septins (SEPT1 to SEPT12 and SEPT14) are classified into four subgroups (SEPT3, SEPT2, SEPT7, and SEPT6) based on sequence homology and coiled-coil domains (Macara et al., 2002; Kinoshita, 2003b). (C) Structure of the SEPT2-6-7 complex. Two copies of each septin are symmetrically arranged (SEPT7-6-2-2-6-7) to generate a hexamer by alternating N- and C-termini (NC) and G-interface (GTP-binding domain) (Sirajuddin et al., 2007). (D) Structure of the SEPT2-6-7-9 complex (Sandrock et al., 2011; Kim et al., 2011). (E) Binding preferences of individual septins to other septins (Sandrock et al., 2011).