M. Mavrakis

The paper identifies a transmembrane domain in septins from C. elegans and primates, showing it is required for membrane association and tissue integrity.

This study shows that human septins form octamer-based filaments that mediate actin-membrane anchoring, as demonstrated through various imaging and biophysical techniques.

The paper identifies a MAP-like motif in Sept9 isoform 1 that drives septin-microtubule interaction and shows how HNA mutations disrupt this association.

The paper introduces 4polar-STORM, a new microscopy method that combines STORM with polarization-resolved imaging to determine single molecule localization and orientation in cells, revealing bimodal actin filament orientations in lamellipodia.

This study isolates recombinant human septin octamers with distinct SEPT9 isoforms and shows they form filament assemblies and bind actin filaments.

This study shows membrane binding enables fly septins to form ordered filamentous arrays, with C-terminal regions required for stacking.