ArticleMolecular biology of the cell2015
Functional insight into the role of Orc6 in septin complex filament formation in Drosophila.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- HumanizedGenetics · 2020Article
- Structural basis of DNA replication origin recognition by human Orc6 protein binding with DNA.Nucleic acids research · 2020Article
- Control of septin filament flexibility and bundling by subunit composition and nucleotide interactions.Molecular biology of the cell · 2018Article
- Spatial effects - site-specific regulation of actin and microtubule organization by septin GTPases.Journal of cell science · 2018Review
- Phosphorylation of Pnut in the Early Stages ofG3 (Bethesda, Md.) · 2018Article
- Nonreplicative functions of the origin recognition complex.Nucleus (Austin, Tex.) · 2018Review
- The Role of Pnut and its Functional Domains inRussian journal of genetics. Applied research · 2017Article
- The Arf activator GBF1 localizes to plasma membrane sites involved in cell adhesion and motility.Cellular logistics · 2017Article
- GTPase domain driven dimerization of SEPT7 is dispensable for the critical role of septins in fibroblast cytokinesis.Scientific reports · 2016Article
- Regulation of Store-Operated CaFrontiers in cell and developmental biology · 2016Article
- Drosophila model of Meier-Gorlin syndrome based on the mutation in a conserved C-Terminal domain of Orc6.American journal of medical genetics. Part A · 2015Article
- [Functional Characterization of Septin Complexes].Molekuliarnaia biologiiaReview
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
Septins belong to a family of polymerizing GTP-binding proteins that are important for cytokinesis and other processes that involve spatial organization of the cell cortex. We reconstituted a recombinant Drosophila septin complex and compared activities of the wild-type and several mutant septin complex variants both in vitro and in vivo. We show that Drosophila septin complex functions depend on the intact GTP-binding and/or hydrolysis domains of Pnut, Sep1, and Sep2. The presence of the functional C-terminal domain of septins is required for the integrity of the complex. Drosophila Orc6 protein, the smallest subunit of the origin recognition complex (ORC), directly binds to septin complex and facilitates septin filament formation. Orc6 forms dimers through the interactions of its N-terminal, TFIIB-like domains. This ability of the protein suggests a direct bridging role for Orc6 in stimulating septin polymerization in Drosophila. Studies reported here provide a functional dissection of a Drosophila septin complex and highlight the basic conserved and divergent features among metazoan septin complexes.
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