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Updated: May 17, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
Published on: July 28, 2022
Posttranslational modifications and assembly of septin heteropolymers and higher-order structures
Yainitza Hernández-Rodríguez1, Michelle Momany
1Department of Plant Biology, 2502 Miller Plant Sciences, University of Georgia, Athens, GA 30602-7271, USA.
Abstract:
Septins are cytoskeletal elements that contain a highly conserved canonical G domain flanked by more divergent N- and C-termini. Septin monomers form heteropolymers that in turn associate into a variety of higher-order structures. SUMOylation, acetylation and phosphorylation of septins have all been reported; however, there are no examples of residues that are universally modified suggesting that posttranslational modifications of septins evolved relatively recently. Within the conserved G domain, posttranslational modifications cluster in regions near the G interface, consistent with roles in modulating heteropolymer assembly. Within the highly diverged N- and C-termini, posttranslational modifications are scattered randomly, consistent with roles in modulating assembly of higher-order structures that are unique to individual organisms.
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