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.

journal_name

Curr Opin Microbiol

authors

Hernández-Rodríguez Y,Momany M

doi

10.1016/j.mib.2012.09.007

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

660-8

issue

6

eissn

1369-5274

issn

1879-0364

pii

S1369-5274(12)00123-3

journal_volume

15

pub_type

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