Drosophila Filamin encoded by the cheerio locus is a component of ovarian ring canals

Sokol, Nicholas S.; Cooley, Lynn

doi:10.1016/s0960-9822(99)80502-8

Cited by 104 publications

(144 citation statements)

References 52 publications

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“…Ring canals are stable cytoplasmic bridges between neighbouring germ cells that are formed from an arrested cleavage furrow by addition of several actin-binding proteins (Mahowald, 1971;Robinson et al, 1997;Sokol and Cooley, 1999). At stage 10-11 of oogenesis, actin struts form 'cages' around the nurse cell nuclei and are thought to hold these nuclei in place during the pumping of cytoplasmic content of the nurse cells into the oocyte (Guild et al, 1997).…”

Section: Resultsmentioning

confidence: 99%

Contribution of sequence variation inDrosophilaactins to their incorporation into actin-based structures in vivo

Röper

Mao

Brown

2005

Journal of Cell Science

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Actin is a highly conserved protein important for many cellular functions including motility, contraction in muscles and intracellular transport. Many eukaryotic genomes encode multiple actin protein isoforms that differ from each other by only a few residues. We addressed whether the sequence differences between actin paralogues in one species affect their ability to integrate into the large variety of structures generated by filamentous actin. We thus ectopically expressed all six Drosophila actins as fusion proteins with green fluorescent protein (GFP) in a variety of embryonic, larval and adult fly tissues. We found that each actin was able to integrate into most actin structures analysed. For example, in contrast to studies in mammalian cells, the two Drosophila cytoplasmic actins were incorporated into muscle sarcomeres. However, there were differences in the efficiency with which each actin was incorporated into specific actin structures. The most striking difference was observed within the Z-lines of the sarcomeres: one actin was specifically excluded and we mapped this feature to one or both of two residues within the C-terminal half of the protein. Thus, in Drosophila, the primary sequence of different actins does affect their ability to incorporate into actin structures, and so specific GFPactins may be used to label certain actin structures particularly well.

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Section: Resultsmentioning

confidence: 99%

Contribution of sequence variation inDrosophilaactins to their incorporation into actin-based structures in vivo

Röper

Mao

Brown

2005

Journal of Cell Science

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“…Hemocyte smears were allowed to dry, and then were fixed in 4% paraformaldehyde for 10 min, washed in PBS, and blocked for 30 min in 10% normal goat serum, then incubated overnight with the primary antibody. Staining with Filamin antibody (20) was used to outline F-actin in the cell. Filamin antibody was used at a 1:2,000 dilution and the Dorsal antibody (33) was diluted 1:1.…”

Section: Methodsmentioning

confidence: 99%

“…To examine phagocytic cells, we stained hemocytes with an antibody that recognizes the Drosophila homologue of Filamin (20), an actin-binding protein that has been used to label mammalian macrophages (21,22). Most Blood cells, lymph glands 4.3 Ϯ 1.0 44 Ϫ Antibiotic-treated larvae were grown on minimal medium (see Materials and Methods).…”

Section: Dif and Dorsal Proteins Are Required For Blood Cell Survivalmentioning

confidence: 99%

Rel/NF-κB double mutants reveal that cellular immunity is central to Drosophila host defense

Matova

Anderson²

2006

Proc. Natl. Acad. Sci. U.S.A.

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Studies on Drosophila immunity have focused on the humoral response, whereas less is known about the Drosophila cellular immunity. Here we show that mutants that lack the Drosophila Rel͞NF-B proteins Dorsal and Dif have very few blood cells, are constitutively infected by opportunistic microbes, and die from infection as larvae. When the double mutants are grown in microbe-free conditions, the animals are rescued from chronic infection and many survive to adult stages. Thus, Dif and Dorsal are required for survival because they protect the animal from infection by microbes from the environment. Specific expression of Dif or dorsal in the blood cell lineage is sufficient to restore blood cell number, clear microbes, and allow survival to the adult stage. These findings demonstrate that the cellular immune response is essential for the ability of Drosophila to survive in their standard laboratory environment, and that Dif and Dorsal control crucial aspects of the cellular immune response, including blood cell survival and the ability to fight off microbial infection.innate immunity ͉ macrophages ͉ phagocytosis ͉ humoral immune response

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“…The growth of ring canals is dependent on a robust and dynamic F-actin cytoskeleton. Analysis of cytoskeletal genes demonstrated the importance of the F-actin cytoskeleton for ring canal growth and integrity: loss of ring canal F-actin in cheerio mutants results in destabilized ring canals Li et al 1999;Sokol and Cooley 1999) and loss of F-actin polymerization activity when components of the Arp2/3 complex are mutated results in ring canals that fail to grow and also lack structural stability .…”

mentioning

confidence: 99%

Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase

2015

Self Cite

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The Drosophila Kelch protein is required to organize the ovarian ring canal cytoskeleton. Kelch binds and cross-links F-actin in vitro, and it also functions with Cullin 3 (Cul3) as a component of a ubiquitin E3 ligase. How these two activities contribute to cytoskeletal remodeling in vivo is not known. We used targeted mutagenesis to investigate the mechanism of Kelch function. We tested a model in which Cul3-dependent degradation of Kelch is required for its function, but we found no evidence to support this hypothesis. However, we found that mutant Kelch deficient in its ability to interact with Cul3 failed to rescue the kelch cytoskeletal defects, suggesting that ubiquitin ligase activity is the principal activity required in vivo. We also determined that the proteasome is required with Kelch to promote the ordered growth of the ring canal cytoskeleton. These results indicate that Kelch organizes the cytoskeleton in vivo by targeting a protein substrate for degradation by the proteasome.

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Drosophila Filamin encoded by the cheerio locus is a component of ovarian ring canals

Cited by 104 publications

References 52 publications

Contribution of sequence variation inDrosophilaactins to their incorporation into actin-based structures in vivo

Contribution of sequence variation inDrosophilaactins to their incorporation into actin-based structures in vivo

Rel/NF-κB double mutants reveal that cellular immunity is central to Drosophila host defense

Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase

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