Characterization and distribution of NKD, a receptor for Drosophila tachykinin-related peptide 6

Poels, Jeroen; Birse, Ryan T.; Nachman, Ronald J.; Fichna, Jakub; Janecka, Anna; Broeck, Jozef Vanden; Nässel, Dick R.

doi:10.1016/j.peptides.2008.10.012

Cited by 76 publications

(82 citation statements)

References 39 publications

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“…We observed that ITPL acted only on BNGR-A24 and not on BNGR-A32 or -A33, indicating that these three BNGRs may have different modes of recognition for ITPL. The situation is similar to that reported for DTKR and NKD recognition and activation by TRPs in D. melanogaster; DTKR recognizes all six TKPs (35), whereas only one isoform of the six TRPs can activate NKD (36). In this context, BNGR-A24, -A32, and -A33 may also show selectivity for B. mori TRPs.…”

Section: Comparison Of Bngr-a2 and -A34 As Itp Receptors-supporting

confidence: 84%

Identification and Characterization of Receptors for Ion Transport Peptide (ITP) and ITP-like (ITPL) in the Silkworm Bombyx mori

Nagai

Mabashi-Asazuma

Nagasawa

et al. 2014

Journal of Biological Chemistry

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Background: Ion transport peptide (ITP) and ITP-like (ITPL) are crustacean hyperglycemic hormone family peptides in insects. Results: Receptors for ITP and ITPL were screened from orphan Bombyx neuropeptide G protein-coupled receptors (BNGRs). Conclusion: BNGR-A2 and -A34 act as ITP receptors, whereas BNGR-A24 functions as an ITPL receptor. Significance: Receptor identifications provide further understandings of biological events by this neuropeptide superfamily.

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Section: Comparison Of Bngr-a2 and -A34 As Itp Receptors-supporting

confidence: 84%

Identification and Characterization of Receptors for Ion Transport Peptide (ITP) and ITP-like (ITPL) in the Silkworm Bombyx mori

Nagai

Mabashi-Asazuma

Nagasawa

et al. 2014

Journal of Biological Chemistry

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“…Indeed, of the five crustacean pyrokinins we tested [FSPRLamide, CabPK1, CabPK2, PevPK1 and PevPK2 (Ma et al, 2008;Saideman et al, 2007;Torfs et al, 2000)], only one had any effects, suggesting that the receptor in the lobster heart is much more constrained than the receptor that mediates the effects of pyrokinins in the crab stomatogastric system. Such differences in receptor specificity have been seen, for example, in Drosophila, in which one receptor for tachykinin-related peptides is highly specific, responding only to a single isoform, whereas a second receptor is less specific (Poels et al, 2009). Whether this is a difference in the two species or in the receptors in the two parts of the nervous system is not clear from this study alone [but see our companion article (Dickinson et al, 2015)].…”

Section: Discussionmentioning

confidence: 77%

Distinct or shared actions of peptide family isoforms: I. Peptide-specific actions of pyrokinins in the lobster cardiac neuromuscular system

Dickinson

Sreekrishnan

Kwiatkowski

et al. 2015

Journal of Experimental Biology

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Although the crustacean heart is modulated by a large number of peptides and amines, few of these molecules have been localized to the cardiac ganglion itself; most appear to reach the cardiac ganglion only by hormonal routes. Immunohistochemistry in the American lobster Homarus americanus indicates that pyrokinins are present not only in neuroendocrine organs ( pericardial organ and sinus gland), but also in the cardiac ganglion itself, where pyrokinin-positive terminals were found in the pacemaker cell region, as well as surrounding the motor neurons. Surprisingly, the single pyrokinin peptide identified from H. americanus, FSPRLamide, which consists solely of the conserved FXPRLamide residues that characterize pyrokinins, did not alter the activity of the cardiac neuromuscular system. However, a pyrokinin from the shrimp Litopenaeus vannamei [ADFAFNPRLamide, also known as Penaeus vannamei pyrokinin 2 (PevPK2)] increased both the frequency and amplitude of heart contractions when perfused through the isolated whole heart. None of the other crustacean pyrokinins tested (another from L. vannamei and two from the crab Cancer borealis) had any effect on the lobster heart. Similarly, altering the PevPK2 sequence either by truncation or by the substitution of single amino acids resulted in much lower or no activity in all cases; only the conservative substitution of serine for alanine at position 1 resulted in any activity on the heart. Thus, in contrast to other systems (cockroach and crab) in which all tested pyrokinins elicit similar bioactivities, activation of the pyrokinin receptor in the lobster heart appears to be highly isoform specific.

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“…These differences in the signaling properties of these two related receptors are not without precedent. For example, in Drosophila, the tachykinin receptors encoded by CG7887 and CG6515, show fundamental differences in peptide sensitivity, β-arrestin associations, and tissue distributions (Birse et al, 2006;Poels et al, C. E. Hector and others 2009). In mammals, the two different CRF receptors, which are highly related to the diuretic hormone receptors discussed here, also show similar differences in receptor properties.…”

Section: Discussionmentioning

confidence: 99%

Functional differences between two CRF-related diuretic hormone receptors in Drosophila

Hector

Bretz

Zhao

et al. 2009

Journal of Experimental Biology

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SUMMARYIn Drosophila, two related G-protein-coupled receptors are members of the corticotropin releasing factor (CRF) receptor subfamily. We have previously reported that one of these receptors, encoded by CG8422 is a functional receptor for a diuretic hormone, DH 44 . Here, we report that the other CRF receptor subfamily member, encoded by CG12370, is also a receptor for the DH 44 neuropeptide. The lines of evidence to support this identification include increases in cAMP levels due to CG12370 receptor activation and the recruitment of β-arrestin-GFP to the plasma membrane in response to DH 44 application. We compared these features of the receptors DH44-R2 (encoded by CG12370) and DH44-R1 (encoded by CG8422) and found fundamental differences in signaling, association with the arrestins, and peptide sensitivity. We found that the sensitivity of DH44-R2 to the DH 44 peptide is lower than that of DH44-R1, specifically an estimated EC 50 of 7.98E-07 mol l -1 for DH 44 by DH44-R2 to an EC 50 of 5.12E-09 mol l -1 by DH44-R1 and found that previous reports on the sensitivity of the tubule to DH 44 is in agreement with our measurements of DH44-R2 sensitivity. We employed a specific RNAi construct to selectively knock-down DH44-R2 expression and this led to heightened sensitivity to osmotic challenges. The functional characterization of this diuretic hormone receptor in Drosophila demonstrates a high degree of conservation of CRF-like signaling.

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Characterization and distribution of NKD, a receptor for Drosophila tachykinin-related peptide 6

Cited by 76 publications

References 39 publications

Identification and Characterization of Receptors for Ion Transport Peptide (ITP) and ITP-like (ITPL) in the Silkworm Bombyx mori

Identification and Characterization of Receptors for Ion Transport Peptide (ITP) and ITP-like (ITPL) in the Silkworm Bombyx mori

Distinct or shared actions of peptide family isoforms: I. Peptide-specific actions of pyrokinins in the lobster cardiac neuromuscular system

Functional differences between two CRF-related diuretic hormone receptors in Drosophila

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