PT  - JOURNAL ARTICLE
AU  - Benjamin L. Woods
AU  - Kevin S. Cannon
AU  - Amy S. Gladfelter
TI  - Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling
AID  - 10.1101/2020.05.12.090787
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.05.12.090787
4099  - http://biorxiv.org/content/early/2020/05/13/2020.05.12.090787.1.short
4100  - http://biorxiv.org/content/early/2020/05/13/2020.05.12.090787.1.full
AB  - The curvature of the membrane defines cell shape. Septins are GTP-binding proteins that assemble into heteromeric complexes and polymerize into filaments at areas of micron-scale membrane curvature. An amphipathic helix (AH) domain within the septin complex is necessary and sufficient for septins to preferentially assemble onto micron-scale curvature. Here we report that the non-essential fungal septin, Shs1, also has an AH domain capable of recognizing membrane curvature. In mutants lacking a fully functional Cdc12 AH domain, the Shs1 AH domain becomes essential. Moreover, we find that the Cdc12 AH domain is also important for septin bundling, suggesting multiple functions for septin AH domains.Competing Interest StatementThe authors have declared no competing interest.