ArticleFrontiers in cell and developmental biology2023
Evolutionary degeneration of septins into pseudoGTPases: impacts on a hetero-oligomeric assembly interface.
Article in Frontiers in cell and developmental biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Article
- The novel transcriptional activator Bhr1 combining NTPase and Zn(II)2Cys6 DNA-binding domains controls (hemi-)cellulase response to mannose-rich substrates in the white-rot fungusMicrobiology spectrum · 2026Article
- Interface integrity in septin protofilaments is maintained by an arginine residue conserved from yeast to man.Molecular biology of the cell · 2025Article
- A single septin from a polyextremotolerant yeast recapitulates many canonical functions of septin hetero-oligomers.Molecular biology of the cell · 2024Article
- The Evolutionary Origins and Ancestral Features of Septins.bioRxiv : the preprint server for biology · 2024Article
- Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024Review
- The evolutionary origins and ancestral features of septins.Frontiers in cell and developmental biology · 2024Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
The septin family of eukaryotic proteins comprises distinct classes of sequence-related monomers that associate in a defined order into linear hetero-oligomers, which are capable of polymerizing into cytoskeletal filaments. Like actin and ⍺ and β tubulin, most septin monomers require binding of a nucleotide at a monomer-monomer interface (the septin "G" interface) for assembly into higher-order structures. Like ⍺ and β tubulin, where GTP is bound by both subunits but only the GTP at the ⍺-β interface is subject to hydrolysis, the capacity of certain septin monomers to hydrolyze their bound GTP has been lost during evolution. Thus, within septin hetero-oligomers and filaments, certain monomers remain permanently GTP-bound. Unlike tubulins, loss of septin GTPase activity-creating septin "pseudoGTPases"-occurred multiple times in independent evolutionary trajectories, accompanied in some cases by non-conservative substitutions in highly conserved residues in the nucleotide-binding pocket. Here, we used recent septin crystal structures, AlphaFold-generated models, phylogenetics and
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