title: Posttranslational modifications and assembly of septin heteropolymers and higher-order structures.
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.
authors.affiliation: Department of Plant Biology, 2502 Miller Plant Sciences, University of Georgia, Athens, GA 30602-7271, USA.
authors.forename: Yainitza
authors.initials: Y
authors.lastname: Hernández-Rodríguez
authors.forename: Michelle
authors.initials: M
authors.lastname: Momany
mesh_terms: D000107:Acetylation; D056890:Eukaryota; D010766:Phosphorylation; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational; D058112:Septins / Q000378:metabolism*; D058207:Sumoylation
chemical_list: D058112:Septins