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 Microbioljournal_title
Current opinion in microbiologyauthors
Hernández-Rodríguez Y,Momany Mdoi
10.1016/j.mib.2012.09.007subject
Has Abstractpub_date
2012-12-01 00:00:00pages
660-8issue
6eissn
1369-5274issn
1879-0364pii
S1369-5274(12)00123-3journal_volume
15pub_type
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journal_title:Current opinion in microbiology
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journal_title:Current opinion in microbiology
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journal_title:Current opinion in microbiology
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journal_title:Current opinion in microbiology
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journal_title:Current opinion in microbiology
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journal_title:Current opinion in microbiology
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journal_title:Current opinion in microbiology
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journal_title:Current opinion in microbiology
pub_type: 杂志文章,评审
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