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  • 1
    Online Resource
    Online Resource
    The Drosophila hus1 gene is required for homologous recombination repair during meiosis
    Elsevier BV ; 2009
    In:  Mechanisms of Development Vol. 126, No. 8-9 ( 2009-08), p. 677-686
    Details
    In: Mechanisms of Development, Elsevier BV, Vol. 126, No. 8-9 ( 2009-08), p. 677-686
    Type of Medium: Online Resource
    ISSN: 0925-4773
    URL: Article
    DOI: 10.1016/j.mod.2009.05.004
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2009
    detail.hit.zdb_id: 1466356-9
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  • 2
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    An androgenic gland membrane-anchored gene associated with the crustacean insulin-like androgenic gland hormone
    The Company of Biologists ; 2013
    In:  Journal of Experimental Biology
    Details
    In: Journal of Experimental Biology, The Company of Biologists
    Abstract: Crustacean male sexual differentiation is governed by the androgenic gland (AG) and specifically by the secreted insulin-like AG hormone (IAG), thus far identified in several decapod species including the Australian red claw crayfish Cherax quadricarinatus (termed Cq-IAG). While few insulin-like AG genes have been identified in crustaceans, other AG-specific genes have not been documented until now. In the present study we describe the recent identification of a non-IAG AG-specific transcript obtained from the C. quadricarinatus AG cDNA library. This transcript, termed C. quadricarinatus membrane-anchored AG-specific factor (Cq-MAG), was fully sequenced and found to encode a putative product of 189 amino acids including a signal anchoring peptide. Expression of a recombinant GFP fusion protein lacking the signal anchor encoding sequence dramatically affected recombinant protein localization pattern. While the expression of the deleterious fusion protein was observed throughout most of the cell, the native GFP::Cq-MAG fusion protein was observed mainly surrounding the periphery of the nucleus, demonstrating an ER-like localization pattern. Moreover, co-expressing the wild-type Cq-MAG (fused to GFP) and the Cq-IAG hormone revealed that these peptides indeed co-localize. This study is the first to report a protein specifically associated with the insulin-like androgenic gland hormone in addition to the finding of another AG-specific transcript in crustaceans. Previous knowledge suggests that insulin/insulin-like factor secretion involves tissue-specific transcripts and membrane anchored proteins. On this note, Cq-MAG's tissue specificity, anchoring properties, and intracellular co-localization with Cq-IAG suggest that it may play a role in the processing and secretion of this insulin-like androgenic gland hormone.
    Type of Medium: Online Resource
    ISSN: 1477-9145 , 0022-0949
    URL: Article
    DOI: 10.1242/jeb.080523
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 2013
    detail.hit.zdb_id: 1482461-9
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  • 3
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    Table1.docx
    Frontiers Media SA ; 2022
    In:  Frontiers in Cell and Developmental Biology Vol. 9 ( 2022-1-17)
    Details
    In: Frontiers in Cell and Developmental Biology, Frontiers Media SA, Vol. 9 ( 2022-1-17)
    Abstract: Diversity in cytoskeleton organization and function may be achieved through alternative tubulin isotypes and by a variety of post-translational modifications. The Drosophila genome contains five different β-tubulin paralogs, which may play an isotype tissue-specific function in vivo . One of these genes , the β-tubulin60D gene, which is expressed in a tissue-specific manner, was found to be essential for fly viability and fertility. To further understand the role of the β-tubulin60D gene, we generated new β-tubulin60D null alleles ( β-tubulin60D M ) using the CRISPR/Cas9 system and found that the homozygous flies were viable and fertile. Moreover, using a combination of genetic complementation tests, rescue experiments, and cell biology analyses, we identified Pin 1 , an unknown dominant mutant with bristle developmental defects, as a dominant-negative allele of β-tubulin60D . We also found a missense mutation in the Pin 1 mutant that results in an amino acid replacement from the highly conserved glutamate at position 75 to lysine (E75K). Analyzing the ß -tubulin structure suggests that this E75K alteration destabilizes the alpha-helix structure and may also alter the GTP-Mg 2+ complex binding capabilities. Our results revisited the credence that β-tubulin60D is required for fly viability and revealed for the first time in Drosophila , a novel dominant-negative function of missense β-tubulin60D mutation in bristle morphogenesis.
    Type of Medium: Online Resource
    ISSN: 2296-634X
    URL: Article
    URL: Article
    URL: Article
    DOI: 10.3389/fcell.2021.787976
    DOI: 10.3389/fcell.2021.787976.s001
    DOI: 10.3389/fcell.2021.787976.s002
    Language: Unknown
    Publisher: Frontiers Media SA
    Publication Date: 2022
    detail.hit.zdb_id: 2737824-X
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  • 4
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    Expression of the Drosophila melanogaster GADD45 Homolog (CG11086) Affects Egg Asymmetric Development That Is Mediated by the c-Jun N-Terminal Kinase Pathway
    Oxford University Press (OUP) ; 2007
    In:  Genetics Vol. 177, No. 3 ( 2007-11-01), p. 1691-1702
    Details
    In: Genetics, Oxford University Press (OUP), Vol. 177, No. 3 ( 2007-11-01), p. 1691-1702
    Abstract: The mammalian GADD45 (growth arrest and DNA-damage inducible) gene family is composed of three highly homologous small, acidic, nuclear proteins: GADD45α, GADD45β, and GADD45γ. GADD45 proteins are involved in important processes such as regulation of DNA repair, cell cycle control, and apoptosis. Annotation of the Drosophila melanogaster genome revealed that it contains a single GADD45-like protein (CG11086; D-GADD45). We found that, as its mammalian homologs, D-GADD45 is a nuclear protein; however, D-GADD45 expression is not elevated following exposure to genotoxic and nongenotoxic agents in Schneider cells and in adult flies. We showed that the D-GADD45 transcript increased following immune response activation, consistent with previous microarray findings. Since upregulation of GADD45 proteins has been characterized as an important cellular response to genotoxic and nongenotoxic agents, we aimed to characterize the effect of D-GADD45 overexpression on D. melanogaster development. Overexpression of D-GADD45 in various tissues led to different phenotypic responses. Specifically, in the somatic follicle cells overexpression caused apoptosis, while overexpression in the germline affected the dorsal–ventral polarity of the eggshell and disrupted the localization of anterior–posterior polarity determinants. In this article we focused on the role of D-GADD45 overexpression in the germline and found that D-GADD45 caused dorsalization of the eggshell. Since mammalian GADD45 proteins are activators of the c-Jun N-terminal kinase (JNK)/p38 mitogen-activated protein kinase (MAPK) signaling pathways, we tested for a genetic interaction in D. melanogaster. We found that eggshell polarity defects caused by D-GADD45 overexpression were dominantly suppressed by mutations in the JNK pathway, suggesting that the JNK pathway has a novel, D-GADD45-mediated, function in the Drosophila germline.
    Type of Medium: Online Resource
    ISSN: 1943-2631
    URL: Article
    DOI: 10.1534/genetics.107.079517
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2007
    detail.hit.zdb_id: 1477228-0
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  • 5
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    Scale‐type‐specific requirement for the mosquito Aedes aegypti Spindle‐F homologue by regulating microtubule organization
    Wiley ; 2022
    In:  Insect Molecular Biology Vol. 31, No. 2 ( 2022-04), p. 216-224
    Details
    In: Insect Molecular Biology, Wiley, Vol. 31, No. 2 ( 2022-04), p. 216-224
    Abstract: Insect epithelial cells contain unique cellular extensions such as bristles, hairs, and scales. In contrast to bristle and hair, which are not divergent in their shape, scale morphology shows high diversity. In our attempt to characterize the role of the insect‐specific gene, Spindle‐F ( spn‐F ), in mosquito development, we revealed a scale‐type specific requirement for the mosquito Aedes aegypti spn‐F homologue. Using CRISPR‐Cas9, we generated Ae‐spn‐F mutants and found that Ae‐spn‐F is an essential gene, but we were able to recover a few adult escapers. These escapers could not fly nor move, and died after 3 to 4 days. We found that in Ae‐spn‐F mutants, only the tip part of the bristle was affected with bulbous with misoriented ribs. We also show that in Ae‐spn‐F mutants, only in falcate scales, which are curved with a sharp or narrowly rounded apex, and not in other scale types, the tip region is strongly affected. Our analysis also revealed that in contrast to Drosophila spn‐F , which show strong defects in both the actin and microtubule (MT) network in the bristle, the Ae‐spn‐F gene is required only for MT organization in scales and bristles. In summary, our results reveal that Ae‐spn‐F is required for shaping tapered epithelial cellular extension structures, namely, the bristle and falcate scales by affecting MT organization.
    Type of Medium: Online Resource
    ISSN: 0962-1075 , 1365-2583
    URL: Issue
    URL: Article
    DOI: 10.1111/imb.v31.2
    DOI: 10.1111/imb.12752
    Language: English
    Publisher: Wiley
    Publication Date: 2022
    detail.hit.zdb_id: 2020348-2
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  • 6
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    Absence of SCAPER causes male infertility in humans and Drosophila by modulating microtubule dynamics during meiosis
    BMJ ; 2021
    In:  Journal of Medical Genetics Vol. 58, No. 4 ( 2021-04), p. 254-263
    Details
    In: Journal of Medical Genetics, BMJ, Vol. 58, No. 4 ( 2021-04), p. 254-263
    Abstract: Mutation in S-phase cyclin A-associated protein rin the endoplasmic reticulum ( SCAPER ) have been found across ethnicities and have been shown to cause variable penetrance of an array of pathological traits, including intellectual disability, retinitis pigmentosa and ciliopathies. Methods Human clinical phenotyping, surgical testicular sperm extraction and testicular tissue staining. Generation and analysis of short spindle 3 ( ssp3 ) ( SCAPER orthologue) Drosophila CAS9-knockout lines. In vitro microtubule (MT) binding assayed by total internal reflection fluorescence microscopy. Results We show that patients homozygous for a SCAPER mutation lack SCAPER expression in spermatogonia (SPG) and are azoospermic due to early defects in spermatogenesis, leading to the complete absence of meiotic cells . Interestingly, Drosophil a null mutants for the ubiquitously expressed ssp3 gene are viable and female fertile but male sterile. We further show that male sterility in ssp3 null mutants is due to failure in both chromosome segregation and cytokinesis. In cells undergoing male meiosis, the MTs emanating from the centrosomes do not appear to interact properly with the chromosomes, which remain dispersed within dividing spermatocytes (SPCs). In addition, mutant SPCs are unable to assemble a normal central spindle and undergo cytokinesis. Consistent with these results, an in vitro assay demonstrated that both SCAPER and Ssp3 directly bind MTs. Conclusions Our results show that SCAPER null mutations block the entry into meiosis of SPG, causing azoospermia. Null mutations in ssp3 specifically disrupt MT dynamics during male meiosis, leading to sterility. Moreover, both SCAPER and Ssp3 bind MTs in vitro. These results raise the intriguing possibility of a common feature between human and Drosophila meiosis.
    Type of Medium: Online Resource
    ISSN: 0022-2593 , 1468-6244
    URL: Article
    DOI: 10.1136/jmedgenet-2020-106946
    RVK:
    WA 15000
    Language: English
    Publisher: BMJ
    Publication Date: 2021
    detail.hit.zdb_id: 2009590-9
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  • 7
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    The Drosophila IKK-related kinase (Ik2) and Spindle-F proteins are part of a complex that regulates cytoskeleton organization during oogenesis
    Springer Science and Business Media LLC ; 2008
    In:  BMC Cell Biology Vol. 9, No. 1 ( 2008-12)
    Details
    In: BMC Cell Biology, Springer Science and Business Media LLC, Vol. 9, No. 1 ( 2008-12)
    Abstract: IkappaB kinases (IKKs) regulate the activity of Rel/NF-kappaB transcription factors by targeting their inhibitory partner proteins, IkappaBs, for degradation. The Drosophila genome encodes two members of the IKK family. Whereas the first is a kinase essential for activation of the NF-kappaB pathway, the latter does not act as IkappaB kinase. Instead, recent findings indicate that Ik2 regulates F-actin assembly by mediating the function of nonapoptotic caspases via degradation of DIAP1. Also, it has been suggested that ik2 regulates interactions between the minus ends of the microtubules and the actin-rich cortex in the oocyte. Since spn-F mutants display oocyte defects similar to those of ik2 mutant, we decided to investigate whether Spn-F could be a direct regulatory target of Ik2. Results We found that Ik2 binds physically to Spn-F, biomolecular interaction analysis of Spn-F and Ik2 demonstrating that both proteins bind directly and form a complex. We showed that Ik2 phosphorylates Spn-F and demonstrated that this phosphorylation does not lead to Spn-F degradation. Ik2 is localized to the anterior ring of the oocyte and to punctate structures in the nurse cells together with Spn-F protein, and both proteins are mutually required for their localization. Conclusion We conclude that Ik2 and Spn-F form a complex, which regulates cytoskeleton organization during Drosophila oogenesis and in which Spn-F is the direct regulatory target for Ik2. Interestingly, Ik2 in this complex does not function as a typical IKK in that it does not direct SpnF for degradation following phosphorylation.
    Type of Medium: Online Resource
    ISSN: 1471-2121
    URL: Article
    DOI: 10.1186/1471-2121-9-51
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2008
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    detail.hit.zdb_id: 2041486-9
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  • 8
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    Recapitulating Actin Module Organization in the Drosophila Oocyte Reveals New Roles for Bristle-Actin-Modulating Proteins
    MDPI AG ; 2021
    In:  International Journal of Molecular Sciences Vol. 22, No. 8 ( 2021-04-13), p. 4006-
    Details
    In: International Journal of Molecular Sciences, MDPI AG, Vol. 22, No. 8 ( 2021-04-13), p. 4006-
    Abstract: The generation of F-actin bundles is controlled by the action of actin-binding proteins. In Drosophila bristle development, two major actin-bundling proteins—Forked and Fascin—were identified, but still the molecular mechanism by which these actin-bundling proteins and other proteins generate bristle actin bundles is unknown. In this study, we developed a technique that allows recapitulation of bristle actin module organization using the Drosophila ovary by a combination of confocal microscopy, super-resolution structured illumination microscopy, and correlative light and electron microscope analysis. Since Forked generated a distinct ectopic network of actin bundles in the oocyte, the additive effect of two other actin-associated proteins, namely, Fascin and Javelin (Jv), was studied. We found that co-expression of Fascin and Forked demonstrated that the number of actin filaments within the actin bundles dramatically increased, and in their geometric organization, they resembled bristle-like actin bundles. On the other hand, co-expression of Jv with Forked increased the length and density of the actin bundles. When all three proteins co-expressed, the actin bundles were longer and denser, and contained a high number of actin filaments in the bundle. Thus, our results demonstrate that the Drosophila oocyte could serve as a test tube for actin bundle analysis.
    Type of Medium: Online Resource
    ISSN: 1422-0067
    URL: Article
    DOI: 10.3390/ijms22084006
    Language: English
    Publisher: MDPI AG
    Publication Date: 2021
    detail.hit.zdb_id: 2019364-6
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  • 9
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    Expanding the Genetic Code of a Photoautotrophic Organism
    American Chemical Society (ACS) ; 2017
    In:  Biochemistry Vol. 56, No. 16 ( 2017-04-25), p. 2161-2165
    Details
    In: Biochemistry, American Chemical Society (ACS), Vol. 56, No. 16 ( 2017-04-25), p. 2161-2165
    Type of Medium: Online Resource
    ISSN: 0006-2960 , 1520-4995
    URL: Article
    URL: Article
    DOI: 10.1021/acs.biochem.7b00131
    DOI: 10.1021/acs.biochem.7b00131.s001
    RVK:
    WA 15000
    Language: English
    Publisher: American Chemical Society (ACS)
    Publication Date: 2017
    detail.hit.zdb_id: 1472258-6
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  • 10
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    DNA Damage Response-mediated Degradation of Ho Endonuclease via the Ubiquitin System Involves Its Nuclear Export
    Elsevier BV ; 2003
    In:  Journal of Biological Chemistry Vol. 278, No. 49 ( 2003-12), p. 48727-48734
    Details
    In: Journal of Biological Chemistry, Elsevier BV, Vol. 278, No. 49 ( 2003-12), p. 48727-48734
    Type of Medium: Online Resource
    ISSN: 0021-9258
    URL: Article
    DOI: 10.1074/jbc.M308671200
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2003
    detail.hit.zdb_id: 2141744-1
    detail.hit.zdb_id: 1474604-9
    SSG: 12
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