Citation for published item:erikD eF nd tykovD wF nd pontesD wF nd xemuritD sF nd uinlnD F nd er¡ ujoD eF F nd hewroD F @PHITA 9fiophysil dissetion of shistosome septins X insights into oligomeriztion nd memrne indingF9D fiohimieFD IQI F ppF WTEIHSF Further information on publisher's website:
Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. the N-and C-terminal interfaces in a nucleotide independent fashion but form heterodimers via the G interface, which are nucleotide dependent. Furthermore, we report for the first time that it is the C-terminus of SmSETP10, rather than the Nterminal polybasic region found in other septins, that mediates its binding to liposomes.Upon binding we observe formation of discrete lipo-protein clusters and higher order septin structures, making our system an exciting model to study interactions of septins with biological membranes.2