ArticleBiomolecules2023
Diversity and Potential Multifunctionality of Archaeal CetZ Tubulin-like Cytoskeletal Proteins.
Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Archaeal Cytoskeletal Protein CetZ1 Influences Assembly of the Motility Machinery.Molecular microbiology · 2026Article
- Article
- Polymer dynamics of Alp7A reveals how two critical concentrations govern assembly of dynamically unstable actin-like proteins.Molecular biology of the cell · 2024Article
- MinD2 modulates cell shape and motility in the archaeonbioRxiv : the preprint server for biology · 2024Article
- On the critical concentration for net assembly of dynamically unstable polymers.bioRxiv : the preprint server for biology · 2024Article
- Extracellular vesicle formation inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- MinD proteins regulate CetZ1 localization inFrontiers in microbiology · 2024Article
- MinD2 modulates cell shape and motility in the archaeonFrontiers in microbiology · 2024Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Tubulin superfamily (TSF) proteins are widespread, and are known for their multifaceted roles as cytoskeletal proteins underpinning many basic cellular functions, including morphogenesis, division, and motility. In eukaryotes, tubulin assembles into microtubules, a major component of the dynamic cytoskeletal network of fibres, whereas the bacterial homolog FtsZ assembles the division ring at midcell. The functions of the lesser-known archaeal TSF proteins are beginning to be identified and show surprising diversity, including homologs of tubulin and FtsZ as well as a third archaea-specific family, CetZ, implicated in the regulation of cell shape and possibly other unknown functions. In this study, we define sequence and structural characteristics of the CetZ family and CetZ1 and CetZ2 subfamilies, identify CetZ groups and diversity amongst archaea, and identify potential functional relationships through analysis of the genomic neighbourhoods of
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