Drosophila morgue influences cell numbers and positions in the embryonic nervous system

Schreader, Barbara A; Wang, Yiqin; Carter, Stephanie; Grigas, Joanna; Nambu, John R.

doi:10.1387/ijdb.092979bs

Cited by 2 publications

(4 citation statements)

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“…While the precise basis of this Morgue-dependent lethality is not clear and may involve novel Morgue actions, given Morgue’s functions in cell differentiation and survival, it is likely that specific developmental processes are disrupted. This lethality contrasts with the viable phenotype of morgue loss-of-function mutants [27] and suggests that proper regulation of Morgue expression is important for animal development. The Morgue over-expression phenotype exhibits dosage-sensitivity as animals heterozygous for P[ da -gal4], P[UAS-Morgue] are fully viable while animals homozygous for one and heterozygous for the other P element exhibit extensive but generally incomplete lethality.…”

Section: Discussionmentioning

confidence: 88%

“…Morgue was further shown to induce caspase-mediated death of cultured insect cells and in vitro assays indicated that Morgue directly associates with SkpA and DIAP1. Loss-of-function morgue mutants exhibit a slight increase in the number of surviving embryonic midline glia as well as alterations in the normal numbers and positions of other glia and neurons [27]. In addition, Morgue has been shown to regulate the circadian response to light [28].…”

Section: Introductionmentioning

confidence: 99%

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Drosophila Morgue Associates with SkpA and Polyubiquitin In Vivo

et al. 2013

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Morgue is a unique ubiquitination protein that influences programmed cell death and circadian rhythms in Drosophila. We have found that over-expression of wild-type Morgue results in organismal lethality. This over-expression phenotype was used as the basis for an in vivo functional assay to investigate the importance of the Morgue zinc finger, F box, Ubiquitin E2 Conjugase Variant (UEV) domain, and active site Glycine residue. Removal of the zinc finger or UEV domain reduced Morgue’s ability to induce lethality and enhance cell death. In contrast, lack of the F box as well as several different substitutions of the active site Glycine did not alter Morgue-induced lethality or cell death enhancement. To further characterize Morgue functions, a Flag:Morgue protein was used to isolate Morgue-associated proteins from whole adult Drosophila. Mass spectrometry analysis of the Morgue-associated proteins identified SkpA as well as a ubiquitin multimer. The identification of SkpA is consistent with previous in vitro studies and further suggests Morgue acts in an SCF-type ubiquitin E3 ligase complex. The identification of poly-ubiquitin was unexpected and this interaction had not been previously identified. The associated poly-ubiquitin was found to exhibit a Lys-48 topology, consistent with distinct functions of Morgue in proteasome-mediated protein turnover. Multiple regions of Morgue were subsequently shown to be required for poly-ubiquitin binding. Overall, Morgue is a novel multi-functional ubiquitin-binding protein.

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Section: Discussionmentioning

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Drosophila Morgue Associates with SkpA and Polyubiquitin In Vivo

et al. 2013

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“…For instance, cell behavior can be intrinsically influenced by the misexpression of a protein (e.g., cadherins, see Tepass et al, 2000) or by an extrinsically applied chemical substance (e.g., cytochalasin B, see Itow & Sekiguchi, 1980). The misexpression of a protein can be caused by a change at the genetic level such as a natural or experimentally induced mutation (e.g., Schreader et al, 2010; Chesebro, 2012) or by an increased temperature.…”

Section: What Causes Helicomery?mentioning

confidence: 99%

“…In the crustacean Artemia sp., spiral segments were produced in the abdomen based on an experimental treatment with mycophenolic acid, which has a cytostatic effect (Hernandorena, 1993). The generation of null-mutants for the morgue gene in Drosophila led, among other effects, to spiral segments in the abdomen of adult flies (Schreader et al, 2010). Since the morgue protein plays a crucial role for the regulation of cell death, its absence in null-mutants affects cell proliferation.…”

Section: Experimental Approachesmentioning

confidence: 99%

Screwed up: Spirality of segments and other iterated structures suggest an underlying principle of seriality in bilaterians

Scholtz

2021

Journal of Morphology

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This review deals with helicomery, that is, the specific malformation of a spiral arrangement of segments and other serial structures. Helicomery was first described in annelid and arthropod body segments. However, corresponding patterns occur in arthropod appendages and other bilaterians with serially arranged body parts, such as tapeworms, nematodes, vertebrates, and probably chitons. The specifics of the spirals such as length, orientation, and handedness are described. Most spirals are dorsal and comprise only a few loops. Helicomery is formed by a shift of cells during development or in adults caused by changes in cell adhesion or mechanical impacts such as lesions. A model for the formation of helicomery is proposed, which is based on medieval church labyrinths. These complex spiral structures are derived from concentric lines by the shift of relatively few tiles. This principle of “small causes, great effect” also applies to “spiral segments,” because helicomery dissolves segmental patterns and questions the concept of segments as distinct structures. The widespread occurrence of helicomery in nonhomologous serial structures might indirectly indicate an underlying principle of seriality among Bilateria.

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Drosophila morgue influences cell numbers and positions in the embryonic nervous system

Cited by 2 publications

References 61 publications

Drosophila Morgue Associates with SkpA and Polyubiquitin In Vivo

Drosophila Morgue Associates with SkpA and Polyubiquitin In Vivo

Screwed up: Spirality of segments and other iterated structures suggest an underlying principle of seriality in bilaterians

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