Vasopressin-like peptide and its receptor function in an indirect diuretic signaling pathway in the red flour beetle

Aikins, Michael J.; Schooley, David A.; Begum, Khurshida; Detheux, Michel; Beeman, Richard W.; Park, Yoonseong

doi:10.1016/j.ibmb.2008.04.006

Cited by 102 publications

(110 citation statements)

References 36 publications

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“…Canton S was used as a wild-type partner in the mating pairs of behavioral tests. Systemic RNAi in the T. castaneum GA1 strain was performed as previously described (8,9,42,43). Two different stages, approximately the fourth to fifth larval stage and early pupal stage, were used for injections of dsRNA.…”

Section: Methodsmentioning

confidence: 99%

Natalisin, a tachykinin-like signaling system, regulates sexual activity and fecundity in insects

Jiang

Lkhagva

Daubnerová

et al. 2013

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

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122

172

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An arthropod-specific peptidergic system, the neuropeptide designated here as natalisin and its receptor, was identified and investigated in three holometabolous insect species: Drosophila melanogaster, Tribolium castaneum, and Bombyx mori. In all three species, natalisin expression was observed in 3-4 pairs of the brain neurons: the anterior dorso-lateral interneurons, inferior contralateral interneurons, and small pars intercerebralis neurons. In B. mori, natalisin also was expressed in two additional pairs of contralateral interneurons in the subesophageal ganglion. Natalisin-RNAi and the activation or silencing of the neural activities in the natalisin-specific cells in D. melanogaster induced significant defects in the mating behaviors of both males and females. Knockdown of natalisin expression in T. castaneum resulted in significant reduction in the fecundity. The similarity of the natalisin C-terminal motifs to those of vertebrate tachykinins and of tachykinin-related peptides in arthropods led us to identify the natalisin receptor. A G protein-coupled receptor, previously known as tachykinin receptor 86C (also known as the neurokinin K receptor of D. melanogaster), now has been recognized as a bona fide natalisin receptor. Taken together, the taxonomic distribution pattern of the natalisin gene and the phylogeny of the receptor suggest that natalisin is an ancestral sibling of tachykinin that evolved only in the arthropod lineage.N europeptides are ancestral signaling molecules that function as cell-cell communication mediators in multicellular organisms. Large numbers of diverse neuropeptides are involved in the control of animal behavior, development, and physiology. Recent genomic approaches have revealed diverse groups of neuropeptides in different taxa, based on similarities in the amino acid sequences to neuropeptides discovered in earlier physiological and anatomical studies (1-4). Sequenced genomes of many insect species (5) provide an opportunity to explore the evolutionary processes of neuropeptides and their receptors. Furthermore, the tools available in biotechnology that are readily applicable in suitable insect model species have advanced our understanding of the functions of neuropeptides. Drosophila melanogaster has been the best model system, allowing functional studies of neuropeptides and their receptors by the use of highly advanced molecular genetic tools and various publicly available resources (6). A number of other insect species, especially those with sequenced genomes, such as Bombyx mori and Tribolium castaneum, also have been used for investigations into the functions of neuropeptide signals, using piggyBac transformation (7) and RNAi (8,9).Previous studies on insect neuropeptides and their G proteincoupled receptors (GPCRs) have described tachykinin-related peptides (TRPs) and two GPCRs as the receptors for the TRPs in D. melanogaster and other insect species (10-14). In vertebrates tachykinin and the TRPs form a group of ancestral neuropeptides that are found in a wide rang...

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Section: Methodsmentioning

confidence: 99%

Natalisin, a tachykinin-like signaling system, regulates sexual activity and fecundity in insects

Jiang

Lkhagva

Daubnerová

et al. 2013

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

Self Cite

122

172

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“…They were discovered from the mammalian posterior pituitary, with the activities of antidiuresis and increasing in blood pressure (vasopressin) or promoting contractions of the estrogen-treated uterus preparations and the ejection of milk from the mammary glands (oxytocin). Insect oxytocin/vasopressin-like peptide, named inotocin, and its receptor were recently identi fi ed and functional characterized in T. castaneum (Staf fl inger et al 2008 ;Aikins et al 2008 ) . However, RNAi (RNA interference) for inotocin and its receptor has resulted in no mortality or abnormal phenotype in T. castaneum (Aikins et al 2008 ) .…”

Section: Neuropeptide Gpcrsmentioning

confidence: 99%

“…Insect oxytocin/vasopressin-like peptide, named inotocin, and its receptor were recently identi fi ed and functional characterized in T. castaneum (Staf fl inger et al 2008 ;Aikins et al 2008 ) . However, RNAi (RNA interference) for inotocin and its receptor has resulted in no mortality or abnormal phenotype in T. castaneum (Aikins et al 2008 ) .…”

Section: Neuropeptide Gpcrsmentioning

confidence: 99%

G Protein-Coupled Receptors as Target Sites for Insecticide Discovery

Bai

Palli

2012

Advanced Technologies for Managing Insect Pests

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“…The conserved cysteine residues in the neurophysin-like domains are underlined and numbered 1-14. The precursors of vasopressin/oxytocin-like peptides from other species include precursors of human vasopressin (Mohr et al, 1985), human oxytocin (Mohr et al, 1985), vasotocin from the lamprey Lethenteron japonicum (Suzuki et al, 1995), an oxytocin-like peptide (SOP) from the urochordate Styela plicata (Ukena et al, 2008), Lys-conopressin from the mollusc Lymnaea stagnalis (Van Kesteren et al, 1992), cephalotocin from the mollusc Octopus vulgaris (Reich, 1992), annetocin from the annelid Eisenia foetida (Oumi et al, 1994) and inotocin from the arthropod (insect) Tribolium castaneum (Aikins et al, 2008;Stafflinger et al, 2008). Also included is a precursor from the nematode Caenorhabditis elegans (GenBank: NP_001033548, GI:86564869) that has not been reported previously in the literature; this precursor contains an unusual putative vasopressin/oxytocin-like peptide comprising just eight residues (CFLNSCPY), which we have named 'nematocin'.…”

Section: P G I C C G P T I G C H I N T Q H T L S 80 241 Tgtatgcgagaaamentioning

confidence: 99%

NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins

Elphick

Rowe

2009

Journal of Experimental Biology

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SUMMARYThe myoactive neuropeptide NGIWYamide was originally isolated from the holothurian (sea cucumber) Apostichopus japonicus but there is evidence that NGIWYamide-like peptides also occur in other echinoderms. Here we report the discovery of a gene in the sea urchin Strongylocentrotus purpuratus that encodes two copies of an NGIWYamide-like peptide: Asn-Gly-Phe-Phe-Phe-(NH 2 ) or NGFFFamide. Interestingly, the C-terminal region of the NGFFFamide precursor shares sequence similarity with neurophysins, carrier proteins hitherto uniquely associated with precursors of vasopressin/oxytocin-like neuropeptides. Thus, the NGFFFamide precursor is the first neurophysin-containing neuropeptide precursor to be discovered that does not contain a vasopressin/oxytocin-like peptide. However, it remains to be determined whether neurophysin acts as a carrier protein for NGFFFamide. The S. purpuratus genome also contains a gene encoding a precursor comprising a neurophysin polypeptide and 'echinotocin' (CFISNCPKGamide) -the first vasopressin/oxytocin-like peptide to be identified in an echinoderm. Therefore, in S. purpuratus there are two genes encoding precursors that have a neurophysin domain but which encode neuropeptides that are structurally unrelated. Furthermore, both NGFFFamide and echinotocin cause contraction of tube foot and oesophagus preparations from the sea urchin Echinus esculentus, consistent with the myoactivity of NGIWYamide in sea cucumbers and the myoactivity of vasopressin/oxytocin-like peptides in other animal phyla. Presumably the NGFFFamide precursor acquired its neurophysin domain following partial or complete duplication of a gene encoding a vasopressin/oxytocin-like peptide, but it remains to be determined when in evolutionary history this occurred.

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Vasopressin-like peptide and its receptor function in an indirect diuretic signaling pathway in the red flour beetle

Cited by 102 publications

References 36 publications

Natalisin, a tachykinin-like signaling system, regulates sexual activity and fecundity in insects

Natalisin, a tachykinin-like signaling system, regulates sexual activity and fecundity in insects

G Protein-Coupled Receptors as Target Sites for Insecticide Discovery

NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins

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