An immunocytochemical study of the FMRFamide neuropeptide gene products in <i>Drosophila</i>

Schneider, Lynne E.; Sun, Eric T.; Garland, Daniel J.; Taghert, Paul H.

doi:10.1002/cne.903370308

Cited by 86 publications

(88 citation statements)

References 41 publications

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“…As shown Fig. 5, dissected wild type 1st instar larval brains have a stereotypical pattern of neuroendocrine cells in the ventral ganglion of the central nervous system that produce the FMRF pre-propeptide (52). Dissected 1st instar larval brains from ctr1A 25 maternal and zygotic mutants also show a similar pattern of FMRF prepropeptide producing neuroendocrine cells within the ventral ganglion without qualitative differences in abundance (Fig.…”

Section: Ctr1a Localizes To the Plasma Membrane And To Intracellular mentioning

confidence: 64%

Drosophila Ctr1A Functions as a Copper Transporter Essential for Development

Turski¹,

Thiele

2007

Journal of Biological Chemistry

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Copper is an essential trace element required by all aerobic organisms as a cofactor for enzymes involved in normal growth, development, and physiology. Ctr1 proteins are members of a highly conserved family of copper importers responsible for copper uptake across the plasma membrane. Mice lacking Ctr1 die during embryogenesis from widespread developmental defects, demonstrating the need for adequate copper acquisition in the development of metazoan organisms via as yet uncharacterized mechanisms. Whereas the fruit fly, Drosophila melanogaster, expresses three Ctr1 genes, ctr1A, ctr1B, and ctr1C, little is known about their protein isoform-specific roles. Previous studies demonstrated that Ctr1B localizes to the plasma membrane and is not essential for development unless flies are severely copper-deficient or are subjected to copper toxicity. Here we demonstrate that Ctr1A also resides on the plasma membrane and is the primary Drosophila copper transporter. Loss of Ctr1A results in copper-remedial developmental arrest at early larval stages. Ctr1A mutants are deficient in the activity of copper-dependent enzymes, including cytochrome c oxidase and tyrosinase. Amidation of Phe-Met-Arg-Pheamides, a group of cardiomodulatory neuropeptide hormones that are matured via the action of peptidylglycine ␣-hydroxylating monooxygenase, is defective in neuroendocrine cells of Ctr1A mutant larvae. Moreover, both the Phe-Met-Arg-Pheamide maturation and heart beat rate defects observed in Ctr1A mutant larvae can be partially rescued by exogenous copper. These studies establish clear physiological distinctions between two Drosophila plasma membrane copper transport proteins and demonstrate that copper import by Ctr1A is required to drive neuropeptide maturation during normal growth and development.

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Section: Ctr1a Localizes To the Plasma Membrane And To Intracellular mentioning

confidence: 64%

Drosophila Ctr1A Functions as a Copper Transporter Essential for Development

Turski¹,

Thiele

2007

Journal of Biological Chemistry

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“…In total, 17 different DrmFMRFamide cell types might exist. 8 Several studies have shown the existence of at least three different enhancers in …”

Section: The Fmrfamide Precursormentioning

confidence: 99%

Peptidomic analysis of the larval Drosophila melanogaster central nervous system by two‐dimensional capillary liquid chromatography quadrupole time‐of‐flight mass spectrometry

et al. 2005

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Peptides are the largest class of signalling molecules found in animals. Nevertheless, in most proteomic studies peptides are overlooked since they literally fall through the mazes of the net. In analogy with proteomics technology, where all proteins expressed in a cell or tissue are analyzed, the peptidomic approach aims at the simultaneous visualization and identification of the whole peptidome of a cell or tissue, i.e. all expressed peptides with their post-translational modifications. In this paper we describe the analysis of the larval fruit fly central nervous system using two-dimensional capillary liquid chromatography/quadrupole time-of-flight tandem mass spectrometry (LC/Q-TOF-MS/MS. Using the central nervous systems of only 50 larval Drosophila as starting material, we identified 38 peptides in a single analysis, 20 of which were not detected in a previous study that reported on the one-dimensional capillary LC/MS/MS analysis of the same tissue. Among the 38 sequenced peptides, some originate from precursors, such as the tachykinin and the IFamide precursor that were entirely missed in the first study. This clearly demonstrates that the two-dimensional capillary LC approach enhances the coverage of the peptidomic analysis.

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“…The Drosophila FMRFamide gene encodes eight neuropeptides, the most abundant of which is DPKQDFMRFamide (Schneider et al, 1993). Many Drosophila GPCRs sensitive to peptides structurally related to FMRFamide have been deorphaned using cell culture assays (Cazzamali and Grimmelikhuijzen, 2002;Nichols, 2006), but their in vivo functions have not been investigated and little is known about their downstream effectors in synapses.…”

Section: Introductionmentioning

confidence: 99%

Peptide-Induced Modulation of Synaptic Transmission and Escape Response inDrosophilaRequires Two G-Protein-Coupled Receptors

Klose¹,

Dason²,

Atwood³

et al. 2010

J. Neurosci.

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Neuropeptides are found in both mammals and invertebrates and can modulate neural function through activation of G-protein-coupled receptors (GPCRS).The precise mechanisms by which many of these GPCRs modulate specific signaling cascades to regulate neural function are not well defined. We used Drosophila melanogaster as a model to examine both the cellular and behavioral effects of DPKQDFMRFamide, the most abundant peptide encoded by the dFMRF gene. We show that DPKQDFMRFamide enhanced synaptic transmission through activation of two G-protein-coupled receptors, Fmrf Receptor (FR) and Dromyosupressin Receptor-2 (DmsR-2). The peptide increased both the presynaptic Ca 2ϩ response and the quantal content of released transmitter. Peptide-induced modulation of synaptic function could be abrogated by depleting intracellular Ca 2ϩ stores or by interfering with Ca 2ϩ release from the endoplasmic reticulum through disruption of either the ryanodine receptor or the inositol 1,4,5-trisphosphate receptor. The peptide also altered behavior. Exogenous DPKQDFMRFamide enhanced fictive locomotion; this required both the FR and DmsR-2. Likewise, both receptors were required for an escape response to intense light exposure. Thus, coincident detection of a peptide by two GPCRs modulates synaptic function through effects of Ca 2ϩ -induced Ca 2ϩ release, and we hypothesize that these mechanisms are involved in behavioral responses to environmental stress.

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An immunocytochemical study of the FMRFamide neuropeptide gene products in Drosophila

Cited by 86 publications

References 41 publications

Drosophila Ctr1A Functions as a Copper Transporter Essential for Development

Drosophila Ctr1A Functions as a Copper Transporter Essential for Development

Peptidomic analysis of the larval Drosophila melanogaster central nervous system by two‐dimensional capillary liquid chromatography quadrupole time‐of‐flight mass spectrometry

Peptide-Induced Modulation of Synaptic Transmission and Escape Response inDrosophilaRequires Two G-Protein-Coupled Receptors

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