Characterization and spatial distribution of the ELAV protein during <i>Drosophila melanogaster</i> development

Robinow, Steven; White, K. Andrew

doi:10.1002/neu.480220503

Cited by 483 publications

(292 citation statements)

References 47 publications

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“…2 A). The neuronal identity of all cells in culture at this time was confirmed by immunohistochemical staining for ELAV, a neuron-specific nuclear marker (Robinow and White, 1991) (data not shown). Cells expressing ␤gal could easily be identified within the field of neurons (Fig.…”

Section: Y Provides a Marker For Kenyon Cells In Dissociated Cell mentioning

confidence: 75%

The Steroid Hormone 20-Hydroxyecdysone Enhances Neurite Growth ofDrosophilaMushroom Body Neurons Isolated during Metamorphosis

1998

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Mushroom bodies (MBs) are symmetrically paired neuropils in the insect brain that are of critical importance for associative olfactory learning and memory. In Drosophila melanogaster, the MB intrinsic neurons (Kenyon cells) undergo extensive reorganization at the onset of metamorphosis. A phase of rapid axonal degeneration without cell death is followed by axonal regeneration. This re-elaboration occurs as levels of the steroid hormone 20-hydroxyecdysone (20E) are rising during the pupal stage. Based on the known role of 20E in directing many features of CNS remodeling during insect metamorphosis, we hypothesized that the outgrowth of MB axonal processes is promoted by 20E. Using a GAL4 enhancer trap line (201Y) that drives MB-restricted reporter gene expression, we identified Kenyon cells in primary cultures dissociated from early pupal CNS. Paired cultures derived from single brains isolated before the 20E pupal peak were incubated in medium with or without 20E for 2-4 d. Morphometric analysis demonstrated that MB neurons exposed to 20E had significantly greater total neurite length and branch number compared with that of MB neurons grown without hormone. The relationship between branch number and total neurite length remained constant regardless of hormone treatment in vitro, suggesting that 20E enhances the rate of outgrowth from pupal MB neurons in a proportionate manner and does not selectively increase neuritic branching. These results implicate 20E in enhancing axonal outgrowth of Kenyon cells to support MB remodeling during metamorphosis.

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Section: Y Provides a Marker For Kenyon Cells In Dissociated Cell mentioning

confidence: 75%

The Steroid Hormone 20-Hydroxyecdysone Enhances Neurite Growth ofDrosophilaMushroom Body Neurons Isolated during Metamorphosis

1998

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“…To uncover whether either one of these activities can also support longevity, we determined the lifespan of male flies overexpressing CG14207 (strong refolder) and HSP67BC (strong anti‐aggregation) using elav‐GAL4 or ey‐GAL4 promoters. Elav‐GAL4 drives expression in the central and peripheral nervous systems (Robinow & White, 1991). The ey‐GAL4 driver, which is traditionally used for eye‐specific expression, also induces expression in the rest of the body ( flyatlas http://www.flyatlas.org).…”

Section: Resultsmentioning

confidence: 99%

Specific protein homeostatic functions of small heat‐shock proteins increase lifespan

et al. 2015

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SummaryDuring aging, oxidized, misfolded, and aggregated proteins accumulate in cells, while the capacity to deal with protein damage declines severely. To cope with the toxicity of damaged proteins, cells rely on protein quality control networks, in particular proteins belonging to the family of heat‐shock proteins (HSPs). As safeguards of the cellular proteome, HSPs assist in protein folding and prevent accumulation of damaged, misfolded proteins. Here, we compared the capacity of all Drosophila melanogaster small HSP family members for their ability to assist in refolding stress‐denatured substrates and/or to prevent aggregation of disease‐associated misfolded proteins. We identified CG14207 as a novel and potent small HSP member that exclusively assisted in HSP70‐dependent refolding of stress‐denatured proteins. Furthermore, we report that HSP67BC, which has no role in protein refolding, was the most effective small HSP preventing toxic protein aggregation in an HSP70‐independent manner. Importantly, overexpression of both CG14207 and HSP67BC in Drosophila leads to a mild increase in lifespan, demonstrating that increased levels of functionally diverse small HSPs can promote longevity in vivo.

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“…During eye development, although SPI is not necessary for the primary induction of the photoreceptor R8, it is required for the subsequent recruitment of R1 to R7. Given that photoreceptors R1 to R8 express ELAV (22) (Fig. 3C) and that R1 and R6 express BAR (23) (Fig.…”

Section: Frc Is Localized To a Subset Of Golgi Units Distinct From Thosementioning

confidence: 99%

Distinct functional units of the Golgi complex in Drosophila cells

Yano

Yamamoto-Hino

Abe

et al. 2005

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

103

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A striking variety of glycosylation occur in the Golgi complex in a protein-specific manner, but how this diversity and specificity are achieved remains unclear. Here we show that stacked fragments (units) of the Golgi complex dispersed in Drosophila imaginal disk cells are functionally diverse. The UDP-sugar transporter FRINGE-CONNECTION (FRC) is localized to a subset of the Golgi units distinct from those harboring SULFATELESS (SFL), which modifies glucosaminoglycans (GAGs), and from those harboring the protease RHOMBOID (RHO), which processes the glycoprotein SPITZ (SPI). Whereas the glycosylation and function of NOTCH are affected in imaginal disks of frc mutants, those of SPI and of GAG core proteins are not, even though FRC transports a broad range of glycosylation substrates, suggesting that Golgi units containing FRC and those containing SFL or RHO are functionally separable. Distinct Golgi units containing FRC and RHO in embryos could also be separated biochemically by immunoisolation techniques. We also show that Tn-antigen glycan is localized only in a subset of the Golgi units distributed basally in a polarized cell. We propose that the different localizations among distinct Golgi units of molecules involved in glycosylation underlie the diversity of glycan modification.fringe connection ͉ glycosylation ͉ posttranslational modification T he pattern of glycosylation is extremely diverse, yet is highly specific to each protein. How can this specificity (and diversity) be achieved? There are Ͼ300 glycosylenzymes in humans and Ͼ100 in Drosophila, but is their enzymatic specificity sufficient to explain the precise modification of all substrates? One possible mechanism that might also contribute to the specific (and diverse) pattern of glycosylation would be the localization͞compartmentalization of glycosylenzymes.The Golgi complex, where protein glycosylation takes place, has been regarded as a single functional unit, consisting of cis-, medial-, and transcisternae in mammalian cells. However, the three-dimensional reconstruction of electron microscopic images of the mammalian Golgi structure has suggested the existence of more than one Golgi stack, with the individual stacks being connected into a ribbon by tubules bridging equivalent cisternae (1). Furthermore, during mitosis, the Golgi cisternae of mammalian cells become fragmented without their disassembly (2, 3). In Drosophila, Golgi cisternae are stacked but are not connected to form a ribbon at the embryonic and pupal stages even during interphase (4, 5), although there has been no evidence to date to indicate functional differences among the Golgi fragments.We previously reported a Drosophila UDP-sugar transporter, FRINGE CONNECTION (FRC), that transports a broad range of UDP-sugars that can be used for the synthesis of various glycans, including N-linked types, GAGs, and mucin types (6, 7). Interestingly, despite its broad specificity, loss-of-function studies have revealed that FRC is selectively required for Notch glycosylation, but not for GA...

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Characterization and spatial distribution of the ELAV protein during Drosophila melanogaster development

Cited by 483 publications

References 47 publications

The Steroid Hormone 20-Hydroxyecdysone Enhances Neurite Growth ofDrosophilaMushroom Body Neurons Isolated during Metamorphosis

The Steroid Hormone 20-Hydroxyecdysone Enhances Neurite Growth ofDrosophilaMushroom Body Neurons Isolated during Metamorphosis

Specific protein homeostatic functions of small heat‐shock proteins increase lifespan

Distinct functional units of the Golgi complex in Drosophila cells

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