The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Identity check. This report concerns Peanut (Pnut), the D. melanogaster protein specified by the supplied UniProt accession P40797, gene pnut, and ORF CG8705: UniProt P40797. Fly-specific biochemical, genetic, and immunolocalization studies independently identify Pnut as a septin, rather than a similarly named protein from another organism. Its experimentally characterized guanine-nucleotide-binding properties agree with the supplied septin, G_SEPTIN and P-loop NTPase domain annotations. The precise P40797–CG8705 cross-reference comes from the supplied UniProt identification; the papers examined primarily use the names pnut and Peanut. (field1996apurifieddrosophila pages 1-2, huijbregts2009drosophilaorc6facilitates pages 1-2, founounou2013septinsregulatethe pages 2-3)
Primary molecular role. Pnut is a membrane-associated, polymerizing cytoskeletal scaffold, not a transporter or a conventional metabolic enzyme. Together with Sep2 and Sep1, it forms a six-subunit septin complex, commonly represented Pnut–Sep2–Sep1–Sep1–Sep2–Pnut, that can assemble into higher-order filaments. The purified embryonic complex carries approximately one bound guanine nucleotide per septin polypeptide and binds and hydrolyzes added GTP. Thus, GTP is the relevant biochemical substrate for the complex, while its principal established cellular output is spatial organization of the cortex, cleavage furrows and associated actomyosin machinery. The cited experiments do not establish an isolated-Pnut catalytic rate or demonstrate that Pnut is the sole hydrolyzing subunit. (field1996apurifieddrosophila pages 1-2, akhmetova2018phosphorylationofpnut pages 1-7, huijbregts2009drosophilaorc6facilitates pages 1-2)
Pnut’s C-terminal coiled-coil region helps assemble the Sep1/Sep2 complex and engage Orc6, the origin-recognition-complex subunit with an additional cytokinetic role. Pnut coiled-coil deletions disrupt septin-complex incorporation; particular leucine substitutions retain incorporation but markedly weaken Orc6 binding. Orc6 increases the assembled complex’s GTPase activity and promotes filament formation under the tested conditions. These findings support a structural and regulatory function for Pnut within a multiprotein assembly, rather than an independently established Orc6-controlled reaction catalyzed by purified Pnut alone. (huijbregts2009drosophilaorc6facilitates pages 1-2, huijbregts2009drosophilaorc6facilitates pages 4-5)
The following evidence map distinguishes direct Pnut experiments from conclusions about its assembled complex and from newer pathway-level findings.
| Molecular/cellular function | Direct evidence | Evidence study (year, DOI/URL) | Limitations |
|---|---|---|---|
| Pnut–Sep2–Sep1 septin complex; guanine-nucleotide binding, GTP hydrolysis, and filament assembly | Immunoaffinity-purified embryonic complex contained Pnut, Sep2, and Sep1 and was inferred to be a heterohexamer with two copies of each subunit. It carried approximately one guanine nucleotide per septin polypeptide, bound and hydrolyzed added GTP, and polymerized into filaments. Pnut therefore functions primarily as a polymerizing septin subunit rather than as a soluble metabolic enzyme. (field1996apurifieddrosophila pages 1-2, akhmetova2018phosphorylationofpnut pages 1-7) | Field et al. (1 May 1996), doi:10.1083/jcb.133.3.605 | GTPase activity was measured for the purified complex, not isolated Pnut; a Pnut-specific turnover rate or substrate specificity beyond guanine nucleotide was not established. The P40797–CG8705 cross-reference derives from the supplied UniProt identity and was not independently demonstrated in this paper. |
| Pnut C-terminal coiled coil: septin-complex assembly, Orc6 interaction, and cortical organization | Recombinant pull-downs showed that deleting Pnut’s coiled-coil region prevented assembly with Sep1/Sep2; leucine substitutions could preserve complex incorporation while strongly reducing Orc6 binding. Orc6 bound the Pnut-containing complex, increased complex GTPase activity, and promoted filament formation. Pnut RNAi in L2 cells caused multinucleation and Orc6 mislocalization. (huijbregts2009drosophilaorc6facilitates pages 1-2, huijbregts2009drosophilaorc6facilitates pages 4-5) | Huijbregts et al. (1 January 2009), doi:10.1091/mbc.e08-07-0754 | Orc6 stimulation applies to the assembled septin complex, not demonstrably to isolated Pnut catalysis. Overexpressed Pnut formed aggregates, and deletion mutants may perturb folding as well as individual interaction surfaces. |
| Cortical furrows and Ran–importin–Anillin-dependent Pnut recruitment | In syncytial embryos, inhibiting Ran impaired pseudocleavage-furrow formation, depth, and persistence and specifically prevented Pnut—but not actin or Anillin—from localizing to furrows. Importin-α/β binding to Anillin blocked the Anillin–Pnut interaction in biochemical assays; RanGTP reversed that inhibition. An Anillin mutant lacking the importin-binding site bypassed the effect of Ran inhibition on furrow ingression. (silvermangavrila2008anillinmediatedtargetingof pages 1-2) | Silverman-Gavrila et al. (September 2008; online 25 June 2008), doi:10.1091/mbc.e08-01-0049 | Establishes regulated recruitment and furrow function, not direct membrane binding by isolated Pnut. Pseudocleavage furrows are transient embryonic structures and do not complete cytokinesis. |
| Maintenance of embryonic cellularization architecture | Maternal Pnut depletion did not prevent initial furrow ingression or initial actin-network assembly, but during fast cellularization F-actin became patchy/punctate, Anillin progressively declined at the front, and gastrulation subsequently failed. Sep1 disappeared from the front whereas Sep2 remained, indicating Pnut-dependent complex organization plus partial septin redundancy. (adam2000evidenceforfunctional pages 10-11, adam2000evidenceforfunctional pages 7-10, adam2000evidenceforfunctional pages 5-7) | Adam et al. (September 2000), doi:10.1091/mbc.11.9.3123 | Residual Sep2 antibody signal may include cross-reactivity with Sep5. The results argue that Pnut maintains later cortical organization, not that it is universally indispensable for every division. |
| Planar epithelial cytokinesis and adherens-junction remodeling | In pnut mutant epidermal cells, the Anillin-positive actomyosin ring contracted slowly, remained anchored at the adherens-junction belt, became oblong, and failed to disengage E-cadherin contacts efficiently. Laser ablation of neighboring junctions relieved tension and rescued junction disengagement/new daughter junction formation in 10/22 cases (45%); E-cadherin overexpression delayed contraction by an additional 3 min ± 30 s. Pnut was required for planar but not orthogonal epithelial divisions. (founounou2013septinsregulatethe pages 11-12, founounou2013septinsregulatethe pages 2-3) | Founounou et al. (11 February 2013), doi:10.1016/j.devcel.2013.01.008 | The phenotype reflects tissue mechanics and the assembled septin system; it does not prove that Pnut alone generates contractile force. Orthogonal divisions can finish without Pnut, demonstrating strong context dependence. |
| C-terminal phosphorylation controls membrane association, complex stability, and viability | Mass spectrometry identified phosphorylation at T509 and S517; phosphorylated Pnut reached up to 40% of total Pnut in the first 2 h of embryogenesis. In mitotic S2 cells, membrane localization occurred in 9.5% of WT (n=74), 69.6–69.7% of non-phosphorylatable T509A/S517A (n=69), and 17.5% of phosphomimetic T509E/S517E cells (n=63). At 29°C, adult survival was 21.7±4.8% for the alanine mutant versus 57.5±9.7% for WT. The phosphomimetic complex was unstable at low salt and formed aggregates/few short filaments. (akhmetova2018phosphorylationofpnut pages 11-16, akhmetova2018phosphorylationofpnut pages 16-20, akhmetova2018phosphorylationofpnut pages 20-24) | Akhmetova et al. (January 2018), doi:10.1534/g3.117.300186 | Glutamate and alanine substitutions only approximate constitutive phosphorylation and dephosphorylation. The responsible kinase/phosphatase was not established, and in-vitro salt conditions do not fully reproduce the embryonic cortex. |
| Rho-regulated membrane recruitment, border-cell surface geometry, and collective migration | Pnut occupied cytoplasmic and membrane pools and was enriched at border-cell–nurse-cell interfaces. Dominant-negative RhoN19 decreased membrane-associated Pnut and increased cytoplasmic puncta; active RhoV14 increased cortical Pnut. Pnut, Sep1, or Sep2 RNAi impaired detachment and migration, while excess Sep1/Sep2 also impaired migration; among clusters that detached after septin perturbation, 30–70% migrated abnormally. Knockdown of one complex member reduced abundance of the others, supporting mutual stabilization. (gabbert2023septinsregulateborder pages 28-37, gabbert2023septinsregulateborder pages 37-42) | Gabbert et al. (August 2023), doi:10.1016/j.devcel.2023.05.017 | Rho manipulation establishes upstream control of localization but not direct Rho–Pnut binding. Myosin and septins colocalized dynamically yet did not measurably recruit one another, so their mechanistic coupling remains unresolved. |
| Anillin-organized anillo-septin pool during contractile-ring closure (recent contextual evidence) | In Drosophila S2-cell deplete-and-rescue experiments, an Anillin allele defective in Rho1-GTP binding and anillo-septin assembly complemented an allele defective in Sticky/Citron-kinase interaction. The results support physically distinct Anillin pools: a Rho1/septin-associated pool involved in contractile-ring closure/shedding and a Sticky-associated pool involved in midbody-ring formation. (chambaud2024heteroalleliccombinationof pages 1-6, chambaud2024heteroalleliccombinationof pages 15-19) | Chambaud, Carim & Hickson (preprint, 22 April 2024), doi:10.1101/2024.04.21.590302 | Contextual, not standalone biochemical proof about Pnut. The experiments manipulate Anillin domains and infer septin-pool behavior from prior Pnut-dependent work; they do not purify Pnut, measure its GTPase activity, or demonstrate a new direct Pnut interaction. It is also a preprint rather than a peer-reviewed 2024 paper in the retrieved evidence set. |
Table: Compact evidence map for the verified Drosophila melanogaster septin Pnut, separating direct biochemical and genetic findings from complex-level inference and recent contextual evidence.
Pnut acts principally inside cells at the plasma-membrane-associated cortex: at dividing-cell cleavage furrows and intercellular bridges, transient embryonic pseudocleavage furrows, and the leading-edge/furrow-canal network of embryonic cellularization. In the developing ovary it also occurs in the cytoplasm and is enriched at the outer interfaces of migrating border cells with nurse cells. These are context-dependent distributions, not evidence that Pnut is secreted or a transmembrane transporter. Antibody staining, tagged-protein imaging, protein depletion and rescue collectively support these sites of action. (adam2000evidenceforfunctional pages 2-3, adam2000evidenceforfunctional pages 4-5, silvermangavrila2008anillinmediatedtargetingof pages 1-2, gabbert2023septinsregulateborder pages 37-42, huijbregts2009drosophilaorc6facilitates pages 1-2)
Pnut is not constitutively membrane-bound. Mass spectrometry identified phosphorylation of its C-terminal T509 and S517 in early embryos; the phosphorylated form reached up to 40% of total Pnut during the first two hours. In mitotic S2 cells, membrane-associated staining occurred in 9.5% of wild-type cells (n = 74), versus 69.6–69.7% with nonphosphorylatable T509A/S517A (n = 69) and 17.5% with phosphomimetic T509E/S517E (n = 63). The alanine mutant also compromised development: survival to adulthood at 29°C was 21.7 ± 4.8%, compared with 57.5 ± 9.7% for the wild-type transgene. Recombinant phosphomimetic complexes were less stable and assembled poorly into long filaments under low-salt conditions. The data indicate that regulated Pnut modification helps control cortical association and septin-assembly dynamics; the responsible kinase was not established, and amino-acid substitutions are imperfect substitutes for native phosphorylation. Akhmetova et al., January 2018. (akhmetova2018phosphorylationofpnut pages 11-16, akhmetova2018phosphorylationofpnut pages 16-20, akhmetova2018phosphorylationofpnut pages 20-24)
Embryonic furrows and Anillin/Ran regulation. Pnut participates in the cortical network that organizes embryonic cellularization. In embryos deprived of maternal Pnut, initial cellularization and early actin assembly still occur, but F-actin at cell bases becomes progressively disorganized during the fast phase; Anillin at the front decreases and subsequent morphogenesis is abnormal. Importantly, Sep1 no longer concentrates at the front, whereas a Sep2-reactive signal remains, demonstrating differential septin dependence rather than a requirement for Pnut in every early furrow event. The Sep2 antibody could also detect Sep5, limiting assignment of the residual signal solely to Sep2. Adam et al., September 2000. (adam2000evidenceforfunctional pages 1-2, adam2000evidenceforfunctional pages 7-10, adam2000evidenceforfunctional pages 11-12)
An experimentally defined recruitment pathway places Pnut downstream of Ran–importin–Anillin in syncytial embryos. Importin-α/β binding to Anillin inhibits Anillin’s interaction with Pnut; RanGTP relieves this inhibition. Perturbing Ran prevents Pnut—but not Anillin or actin—from localizing normally to pseudocleavage furrows and impairs their ingression. An Anillin variant lacking the importin-binding site bypasses the measured effect of Ran inhibition on furrow depth and persistence. This is evidence for regulated Pnut targeting and cortical-furrow organization, not evidence that Pnut itself is an effector GTPase of Ran. Silverman-Gavrila et al., September 2008; published online June 2008. (silvermangavrila2008anillinmediatedtargetingof pages 1-2)
Cytokinesis under epithelial mechanical load. In the fly dorsal-thorax epithelium, Pnut-dependent septin function supports contractile-ring constriction where a planar cleavage furrow must remodel E-cadherin-based adherens junctions. pnut mutant rings constrict more slowly, remain abnormally shaped and attached at the junctional belt, and often fail to disengage neighboring adhesive contacts. Reducing mechanical opposition by laser-ablation of nearby junctions restored disengagement and new daughter-cell junction formation in 10 of 22 trials (45%); E-cadherin overexpression added 3 ± 0.5 minutes of contraction delay. By contrast, orthogonal epithelial divisions can finish without Pnut, although more slowly. The investigators’ force-threshold interpretation is that septin-supported contraction must overcome junctional resistance; the experiments do not show that Pnut itself is a motor or generates force independently of actomyosin. Founounou et al., February 2013. (founounou2013septinsregulatethe pages 1-2, founounou2013septinsregulatethe pages 11-12, founounou2013septinsregulatethe pages 2-3)
Rho signaling and collective migration—recent primary evidence. The 2023 border-cell study identifies a second, non-cytokinetic setting for the Pnut-containing complex. Pnut, Sep1 and Sep2 occur in membrane-associated and cytoplasmic pools, and reducing Sep1 or Sep2 reduces Pnut abundance, consistent with mutually stabilized assemblies. Dominant-negative RhoN19 decreases cortical Pnut, especially at border-cell–nurse-cell contacts, whereas active RhoV14 increases cortical Pnut; opposite changes occur in cytoplasmic septin puncta. RNAi against pnut, Sep1 or Sep2 impairs border-cell detachment and migration. Among perturbed clusters that did detach, 30–70% failed to migrate normally; altered septin abundance also changed cell-surface geometry. Although septins and myosin dynamically colocalize, their knockdowns did not demonstrate that one directly recruits the other. Accordingly, the supported pathway is Rho activity → septin cortical recruitment → appropriate cell-surface organization and collective motility, not proven direct Rho–Pnut binding. Gabbert et al., August 2023. (gabbert2023septinsregulateborder pages 28-37, gabbert2023septinsregulateborder pages 37-42)
2024 mechanistic context. A 2024 preprint using Drosophila S2-cell Anillin separation-of-function alleles reports that Anillin molecules supporting Rho1-dependent septin assembly and those engaging Citron kinase/Sticky can constitute separable functional pools during the transition from contractile ring to midbody ring. Earlier Pnut-depletion experiments cited in that work implicated Pnut in shedding Anillin from the nascent midbody ring. This refines the proposed Rho1–Anillin–septin cytokinesis pathway, but the 2024 experiments principally manipulate Anillin, rather than biochemically assigning a new catalytic or binding activity to Pnut; the source is a preprint. Chambaud, Carim & Hickson, April 2024. (chambaud2024heteroalleliccombinationof pages 1-6, chambaud2024heteroalleliccombinationof pages 15-19)
The most defensible functional annotation is “GTP-binding septin subunit that assembles with other septins into a regulated cortical scaffold supporting furrow architecture, actomyosin-associated cytokinesis and, in border cells, Rho-dependent surface organization and motility.” This integrates purified-complex biochemistry with pnut-specific genetic, imaging and rescue results while retaining an important qualification: Pnut dependence is cell-type and mechanical-context dependent, and complex-level GTP hydrolysis must not be mistaken for a measured Pnut-only enzyme reaction. The fly knockout, RNAi, transgenic-mutant, microscopy and in-vitro reconstitution systems constitute current research implementations; the retrieved evidence establishes experimental model-organism use, not a clinical application. Field et al., May 1996; Adam et al., September 2000; Gabbert et al., August 2023. (field1996apurifieddrosophila pages 1-2, adam2000evidenceforfunctional pages 10-11, gabbert2023septinsregulateborder pages 28-37)
References
(field1996apurifieddrosophila pages 1-2): C. Field, Omayma S. Al-Awar, J. Rosenblatt, M. Wong, B. Alberts, and T. Mitchison. A purified drosophila septin complex forms filaments and exhibits gtpase activity. The Journal of Cell Biology, 133:605-616, May 1996. URL: https://doi.org/10.1083/jcb.133.3.605, doi:10.1083/jcb.133.3.605. This article has 408 citations.
(huijbregts2009drosophilaorc6facilitates pages 1-2): Richard P.H. Huijbregts, Anton Svitin, Monica W. Stinnett, Matthew B. Renfrow, and Igor Chesnokov. Drosophila orc6 facilitates gtpase activity and filament formation of the septin complex. Molecular biology of the cell, 20 1:270-81, Jan 2009. URL: https://doi.org/10.1091/mbc.e08-07-0754, doi:10.1091/mbc.e08-07-0754. This article has 60 citations and is from a domain leading peer-reviewed journal.
(founounou2013septinsregulatethe pages 2-3): Nabila Founounou, Nicolas Loyer, and Roland Le Borgne. Septins regulate the contractility of the actomyosin ring to enable adherens junction remodeling during cytokinesis of epithelial cells. Developmental cell, 24 3:242-55, Feb 2013. URL: https://doi.org/10.1016/j.devcel.2013.01.008, doi:10.1016/j.devcel.2013.01.008. This article has 181 citations and is from a highest quality peer-reviewed journal.
(akhmetova2018phosphorylationofpnut pages 1-7): Katarina Akhmetova, Maxim Balasov, Anton Svitin, Elena Chesnokova, Matthew Renfrow, and Igor Chesnokov. Phosphorylation of pnut in the early stages ofdrosophilaembryo development affects association of the septin complex with the membrane and is important for viability. G3 Genes|Genomes|Genetics, 8:27-38, Jan 2018. URL: https://doi.org/10.1534/g3.117.300186, doi:10.1534/g3.117.300186. This article has 11 citations.
(huijbregts2009drosophilaorc6facilitates pages 4-5): Richard P.H. Huijbregts, Anton Svitin, Monica W. Stinnett, Matthew B. Renfrow, and Igor Chesnokov. Drosophila orc6 facilitates gtpase activity and filament formation of the septin complex. Molecular biology of the cell, 20 1:270-81, Jan 2009. URL: https://doi.org/10.1091/mbc.e08-07-0754, doi:10.1091/mbc.e08-07-0754. This article has 60 citations and is from a domain leading peer-reviewed journal.
(silvermangavrila2008anillinmediatedtargetingof pages 1-2): Rosalind V. Silverman-Gavrila, Karen G. Hales, and Andrew Wilde. Anillin-mediated targeting of peanut to pseudocleavage furrows is regulated by the gtpase ran. Molecular biology of the cell, 19 9:3735-44, Sep 2008. URL: https://doi.org/10.1091/mbc.e08-01-0049, doi:10.1091/mbc.e08-01-0049. This article has 55 citations and is from a domain leading peer-reviewed journal.
(adam2000evidenceforfunctional pages 10-11): Jennifer C. Adam, John R. Pringle, and Mark Peifer. Evidence for functional differentiation among drosophila septins in cytokinesis and cellularization. Molecular biology of the cell, 11 9:3123-35, Sep 2000. URL: https://doi.org/10.1091/mbc.11.9.3123, doi:10.1091/mbc.11.9.3123. This article has 183 citations and is from a domain leading peer-reviewed journal.
(adam2000evidenceforfunctional pages 7-10): Jennifer C. Adam, John R. Pringle, and Mark Peifer. Evidence for functional differentiation among drosophila septins in cytokinesis and cellularization. Molecular biology of the cell, 11 9:3123-35, Sep 2000. URL: https://doi.org/10.1091/mbc.11.9.3123, doi:10.1091/mbc.11.9.3123. This article has 183 citations and is from a domain leading peer-reviewed journal.
(adam2000evidenceforfunctional pages 5-7): Jennifer C. Adam, John R. Pringle, and Mark Peifer. Evidence for functional differentiation among drosophila septins in cytokinesis and cellularization. Molecular biology of the cell, 11 9:3123-35, Sep 2000. URL: https://doi.org/10.1091/mbc.11.9.3123, doi:10.1091/mbc.11.9.3123. This article has 183 citations and is from a domain leading peer-reviewed journal.
(founounou2013septinsregulatethe pages 11-12): Nabila Founounou, Nicolas Loyer, and Roland Le Borgne. Septins regulate the contractility of the actomyosin ring to enable adherens junction remodeling during cytokinesis of epithelial cells. Developmental cell, 24 3:242-55, Feb 2013. URL: https://doi.org/10.1016/j.devcel.2013.01.008, doi:10.1016/j.devcel.2013.01.008. This article has 181 citations and is from a highest quality peer-reviewed journal.
(akhmetova2018phosphorylationofpnut pages 11-16): Katarina Akhmetova, Maxim Balasov, Anton Svitin, Elena Chesnokova, Matthew Renfrow, and Igor Chesnokov. Phosphorylation of pnut in the early stages ofdrosophilaembryo development affects association of the septin complex with the membrane and is important for viability. G3 Genes|Genomes|Genetics, 8:27-38, Jan 2018. URL: https://doi.org/10.1534/g3.117.300186, doi:10.1534/g3.117.300186. This article has 11 citations.
(akhmetova2018phosphorylationofpnut pages 16-20): Katarina Akhmetova, Maxim Balasov, Anton Svitin, Elena Chesnokova, Matthew Renfrow, and Igor Chesnokov. Phosphorylation of pnut in the early stages ofdrosophilaembryo development affects association of the septin complex with the membrane and is important for viability. G3 Genes|Genomes|Genetics, 8:27-38, Jan 2018. URL: https://doi.org/10.1534/g3.117.300186, doi:10.1534/g3.117.300186. This article has 11 citations.
(akhmetova2018phosphorylationofpnut pages 20-24): Katarina Akhmetova, Maxim Balasov, Anton Svitin, Elena Chesnokova, Matthew Renfrow, and Igor Chesnokov. Phosphorylation of pnut in the early stages ofdrosophilaembryo development affects association of the septin complex with the membrane and is important for viability. G3 Genes|Genomes|Genetics, 8:27-38, Jan 2018. URL: https://doi.org/10.1534/g3.117.300186, doi:10.1534/g3.117.300186. This article has 11 citations.
(gabbert2023septinsregulateborder pages 28-37): Allison M. Gabbert, Joseph P. Campanale, James A. Mondo, Noah P. Mitchell, Adele Myers, Sebastian J. Streichan, Nina Miolane, and Denise J. Montell. Septins regulate border cell surface geometry, shape, and motility downstream of rho in drosophila. Developmental Cell, 58:1399-1413.e5, Aug 2023. URL: https://doi.org/10.1016/j.devcel.2023.05.017, doi:10.1016/j.devcel.2023.05.017. This article has 16 citations and is from a highest quality peer-reviewed journal.
(gabbert2023septinsregulateborder pages 37-42): Allison M. Gabbert, Joseph P. Campanale, James A. Mondo, Noah P. Mitchell, Adele Myers, Sebastian J. Streichan, Nina Miolane, and Denise J. Montell. Septins regulate border cell surface geometry, shape, and motility downstream of rho in drosophila. Developmental Cell, 58:1399-1413.e5, Aug 2023. URL: https://doi.org/10.1016/j.devcel.2023.05.017, doi:10.1016/j.devcel.2023.05.017. This article has 16 citations and is from a highest quality peer-reviewed journal.
(chambaud2024heteroalleliccombinationof pages 1-6): Guillaume Chambaud, Sabrya C Carim, and Gilles R X Hickson. Heteroallelic combination of anillin mutants reveals cytoskeletal uncoupling during cytokinesis. bioRxiv, Apr 2024. URL: https://doi.org/10.1101/2024.04.21.590302, doi:10.1101/2024.04.21.590302. This article has 1 citations.
(chambaud2024heteroalleliccombinationof pages 15-19): Guillaume Chambaud, Sabrya C Carim, and Gilles R X Hickson. Heteroallelic combination of anillin mutants reveals cytoskeletal uncoupling during cytokinesis. bioRxiv, Apr 2024. URL: https://doi.org/10.1101/2024.04.21.590302, doi:10.1101/2024.04.21.590302. This article has 1 citations.
(adam2000evidenceforfunctional pages 2-3): Jennifer C. Adam, John R. Pringle, and Mark Peifer. Evidence for functional differentiation among drosophila septins in cytokinesis and cellularization. Molecular biology of the cell, 11 9:3123-35, Sep 2000. URL: https://doi.org/10.1091/mbc.11.9.3123, doi:10.1091/mbc.11.9.3123. This article has 183 citations and is from a domain leading peer-reviewed journal.
(adam2000evidenceforfunctional pages 4-5): Jennifer C. Adam, John R. Pringle, and Mark Peifer. Evidence for functional differentiation among drosophila septins in cytokinesis and cellularization. Molecular biology of the cell, 11 9:3123-35, Sep 2000. URL: https://doi.org/10.1091/mbc.11.9.3123, doi:10.1091/mbc.11.9.3123. This article has 183 citations and is from a domain leading peer-reviewed journal.
(adam2000evidenceforfunctional pages 1-2): Jennifer C. Adam, John R. Pringle, and Mark Peifer. Evidence for functional differentiation among drosophila septins in cytokinesis and cellularization. Molecular biology of the cell, 11 9:3123-35, Sep 2000. URL: https://doi.org/10.1091/mbc.11.9.3123, doi:10.1091/mbc.11.9.3123. This article has 183 citations and is from a domain leading peer-reviewed journal.
(adam2000evidenceforfunctional pages 11-12): Jennifer C. Adam, John R. Pringle, and Mark Peifer. Evidence for functional differentiation among drosophila septins in cytokinesis and cellularization. Molecular biology of the cell, 11 9:3123-35, Sep 2000. URL: https://doi.org/10.1091/mbc.11.9.3123, doi:10.1091/mbc.11.9.3123. This article has 183 citations and is from a domain leading peer-reviewed journal.
(founounou2013septinsregulatethe pages 1-2): Nabila Founounou, Nicolas Loyer, and Roland Le Borgne. Septins regulate the contractility of the actomyosin ring to enable adherens junction remodeling during cytokinesis of epithelial cells. Developmental cell, 24 3:242-55, Feb 2013. URL: https://doi.org/10.1016/j.devcel.2013.01.008, doi:10.1016/j.devcel.2013.01.008. This article has 181 citations and is from a highest quality peer-reviewed journal.