Interspecific comparison of a Drosophila gene encoding FMRFamide- related neuropeptides

Taghert, Paul H.; Schneider, Lynne E.

doi:10.1523/jneurosci.10-06-01929.1990

Cited by 77 publications

(49 citation statements)

References 54 publications

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“…By their positions and patterns, many of the neurons that overexpress dCBP appear identical to previously identified peptidergic neurons (45,56). By using a neuropeptide antibody (PT-2) directed against a specific FMRFamide peptide (67) and an antibody for the neuropeptide biosynthetic enzyme PHM (30), we were able to show that some of these dCBP-overexpressing cells correspond to peptidergic neurons (Fig. 2).…”

Section: Dominantsupporting

confidence: 64%

“…ASH1 was detected by a rabbit polyclonal antibody (71) (affinity purified; kindly provided by Allen Shearn, Johns Hopkins University) at a dilution of 1:40, and dCBP was detected by a chicken polyclonal antibody raised against the CREB binding domain (CBD) of dCBP at a dilution of 1:800. FMRFamide (PT-2) and peptidylglycine-␣-hydroxylating mono-oxygenase (PHM) rabbit polyclonal antibodies (30,67) (kindly provided by Paul Taghert) were used at dilutions of 1:2,000 and 1:500, respectively. Fluorescein anti-rabbit (Vector) and rhodamine anti-chicken (Jackson) secondary antibodies were used at a dilution of 1/200.…”

Section: Methodsmentioning

confidence: 99%

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Functional Interaction between the Coactivator Drosophila CREB-Binding Protein and ASH1, a Member of the Trithorax Group of Chromatin Modifiers

Bantignies

Goodman

Smolik

2000

Molecular and Cellular Biology

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CREB-binding protein (CBP) is a coactivator for multiple transcription factors that transduce a variety of signaling pathways. Current models propose that CBP enhances gene expression by bridging the signalresponsive transcription factors with components of the basal transcriptional machinery and by augmenting the access of transcription factors to DNA through the acetylation of histones. To define the pathways and proteins that require CBP function in a living organism, we have begun a genetic analysis of CBP in flies. We have overproduced Drosophila melanogaster CBP (dCBP) in a variety of cell types and obtained distinct adult phenotypes. We used an uninflated-wing phenotype, caused by the overexpression of dCBP in specific central nervous system cells, to screen for suppressors of dCBP overactivity. Two genes with mutant versions that act as dominant suppressors of the wing phenotype were identified: the PKA-C1/DCO gene, encoding the catalytic subunit of cyclic AMP protein kinase, and ash1, a member of the trithorax group (trxG) of chromatin modifiers. Using immunocolocalization, we showed that the ASH1 protein is specifically expressed in the majority of the dCBP-overexpressing cells, suggesting that these proteins have the potential to interact biochemically. This model was confirmed by the findings that the proteins interact strongly in vitro and colocalize at specific sites on polytene chromosomes. The trxG proteins are thought to maintain gene expression during development by creating domains of open chromatin structure. Our results thus implicate a second class of chromatinassociated proteins in mediating dCBP function and imply that dCBP might be involved in the regulation of higher-order chromatin structure.For proper cellular function and the elaboration of developmental programs, gene expression must be regulated tightly. There is increasing evidence that large transcription complexes, composed of unique combinations of sequence-specific activators and repressors, coactivators, and corepressors, play an important role in determining the temporal and spatial patterns of gene expression (for review, see reference 39).The CREB binding protein (CBP) is one of most extensively characterized coactivator proteins. CBP was first identified through its ability to link the cyclic AMP protein kinase (PKA)-phosphorylated form of CREB to components of the basal transcriptional machinery, including TFIIB (14, 34), , and the RNA polymerase II holoenzyme complex (28,44). CBP is highly related to the adenovirus E1A binding protein p300 (17), and CBP and p300 are considered to be functional homologues (4, 38), although a few differences in their activities have been reported (27). CBP and p300 associate with a wide variety of transcriptional activators in addition to CREB, suggesting that each may serve as a transcriptional integrator of different signaling cascades (reviewed in references 20 and 60). Thus, one model for the function of CBP and p300 is bridging DNA binding transcription factors to components of the b...

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Section: Dominantsupporting

confidence: 64%

Section: Methodsmentioning

confidence: 99%

Functional Interaction between the Coactivator Drosophila CREB-Binding Protein and ASH1, a Member of the Trithorax Group of Chromatin Modifiers

Bantignies

Goodman

Smolik

2000

Molecular and Cellular Biology

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“…C NS and gut tissues were stained in whole mount using procedures similar to those described in Renn et al (1999). Rabbit anti-dPHM was used at a 1:750 dilution (Kolhekar et al, 1997); guinea pig anti-PAP (this recognizes an non-PDF epitope on the proPDF precursor) (Renn et al, 1999) was used at 1:1000; rabbit antiFMRFamide (Taghert and Schneider, 1990) was used at 1:2000; mouse anti-␤GAL (Promega, Madison W I) was used at 1:1000. Secondary antibodies (Jackson ImmunoResearch, West Grove, PA) conjugated with C y3 or Alexa 468 were used at 1:200 or 1:500 dilutions.…”

Section: Methodsmentioning

confidence: 99%

Multiple Amidated Neuropeptides Are Required for Normal Circadian Locomotor Rhythms inDrosophila

et al. 2001

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In Drosophila, the amidated neuropeptide pigment dispersing factor (PDF) is expressed by the ventral subset of lateral pacemaker neurons and is required for circadian locomotor rhythms. Residual rhythmicity in pdf mutants likely reflects the activity of other neurotransmitters. We asked whether other neuropeptides contribute to such auxiliary mechanisms. We used the gal4/UAS system to create mosaics for the neuropeptide amidating enzyme PHM; amidation is a highly specific and widespread modification of secretory peptides in Drosophila. Three different gal4 drivers restricted PHM expression to different numbers of peptidergic neurons. These mosaics displayed aberrant locomotor rhythms to degrees that paralleled the apparent complexity of the spatial patterns. Certain PHM mosaics were less rhythmic than pdf mutants and as severe as per mutants. Additional gal4 elements were added to the weakly rhythmic PHM mosaics. Although adding pdf-gal4 provided only partial improvement, adding the widely expressed tim-gal4 largely restored rhythmicity. These results indicate that, in Drosophila, peptide amidation is required for neuropeptide regulation of behavior. They also support the hypothesis that multiple amidated neuropeptides, acting upstream, downstream, or in parallel to PDF, help organize daily locomotor rhythms.

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“…To evaluate PHM activity in Ctr1A mutant flies, we utilized in situ analysis for the presence of prepro-FMRF peptide and its processed and matured amidated neuropeptides, FMRF-amide-related peptides (50), using an antibody that recognizes the FMRF pre-propeptide (34) and one specific to the amidated form of FMRF-amide-related peptides (34,51). As shown Fig.…”

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

confidence: 99%

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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Interspecific comparison of a Drosophila gene encoding FMRFamide- related neuropeptides

Cited by 77 publications

References 54 publications

Functional Interaction between the Coactivator Drosophila CREB-Binding Protein and ASH1, a Member of the Trithorax Group of Chromatin Modifiers

Functional Interaction between the Coactivator Drosophila CREB-Binding Protein and ASH1, a Member of the Trithorax Group of Chromatin Modifiers

Multiple Amidated Neuropeptides Are Required for Normal Circadian Locomotor Rhythms inDrosophila

Drosophila Ctr1A Functions as a Copper Transporter Essential for Development

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