Structural highlights
Function
SEP10_SCHMA Filament-forming GTP-binding protein. Lacks GTPase activity, which is likely due to absence of an essential threonine residue important for hydrolytic activity in septins. May be involved in membrane remodeling, potentially by its nucleotide-dependent cellular membrane association/dissociation ability (PubMed:24464615). Able to bind to phosphatidylinositol-4,5-bisphosphate (PIP2)-containing giant unilamellar vesicles (GUVs), which serve as a model of biological membranes. Self-assembles into ordered cage-like structures on the vesicle membrane. Binds also to 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS)-containing vesicles suggesting the requirement for negatively charged membranes. Is also able to promote deformation of the GUVs (PubMed:27687162).[1] [2]
References
- ↑ Zeraik AE, Pereira HM, Santos YV, Brandao-Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araujo AP, Demarco R. Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide. J Biol Chem. 2014 Jan 24. PMID:24464615 doi:http://dx.doi.org/10.1074/jbc.M113.525352
- ↑ Zeraik AE, Staykova M, Fontes MG, Nemuraite I, Quinlan R, Araujo AP, DeMarco R. Biophysical dissection of schistosome septins: Insights into oligomerization and membrane binding. Biochimie. 2016 Dec;131:96-105. doi: 10.1016/j.biochi.2016.09.014. Epub 2016 Sep , 26. PMID:27687162 doi:http://dx.doi.org/10.1016/j.biochi.2016.09.014
