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Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy
Synaptic transmission is highly plastic and subject to regulation by a wide variety of neuromodulators and neuropeptides. In the present study, we have examined the role of isoforms of the cytochrome b561 homologue called no extended memory (nemy) in regulation of synaptic strength and plasticity at...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4523183/ https://www.ncbi.nlm.nih.gov/pubmed/26237434 http://dx.doi.org/10.1371/journal.pone.0132548 |
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author | Knight, David Iliadi, Konstantin G. Iliadi, Natalia Wilk, Ronit Hu, Jack Krause, Henry M. Taylor, Paul Moran, Michael F. Boulianne, Gabrielle L. |
author_facet | Knight, David Iliadi, Konstantin G. Iliadi, Natalia Wilk, Ronit Hu, Jack Krause, Henry M. Taylor, Paul Moran, Michael F. Boulianne, Gabrielle L. |
author_sort | Knight, David |
collection | PubMed |
description | Synaptic transmission is highly plastic and subject to regulation by a wide variety of neuromodulators and neuropeptides. In the present study, we have examined the role of isoforms of the cytochrome b561 homologue called no extended memory (nemy) in regulation of synaptic strength and plasticity at the neuromuscular junction (NMJ) of third instar larvae in Drosophila. Specifically, we generated two independent excisions of nemy that differentially affect the expression of nemy isoforms. We show that the nemy (45) excision, which specifically reduces the expression of the longest splice form of nemy, leads to an increase in stimulus evoked transmitter release and altered synaptic plasticity at the NMJ. Conversely, the nemy (26.2) excision, which appears to reduce the expression of all splice forms except the longest splice isoform, shows a reduction in stimulus evoked transmitter release, and enhanced synaptic plasticity. We further show that nemy (45) mutants have reduced levels of amidated peptides similar to that observed in peptidyl-glycine hydryoxylating mono-oxygenase (PHM) mutants. In contrast, nemy (26.2) mutants show no defects in peptide amidation but rather display a decrease in Tyramine β hydroxylase activity (TβH). Taken together, these results show non-redundant roles for the different nemy isoforms and shed light on the complex regulation of neuromodulators. |
format | Online Article Text |
id | pubmed-4523183 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-45231832015-08-06 Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy Knight, David Iliadi, Konstantin G. Iliadi, Natalia Wilk, Ronit Hu, Jack Krause, Henry M. Taylor, Paul Moran, Michael F. Boulianne, Gabrielle L. PLoS One Research Article Synaptic transmission is highly plastic and subject to regulation by a wide variety of neuromodulators and neuropeptides. In the present study, we have examined the role of isoforms of the cytochrome b561 homologue called no extended memory (nemy) in regulation of synaptic strength and plasticity at the neuromuscular junction (NMJ) of third instar larvae in Drosophila. Specifically, we generated two independent excisions of nemy that differentially affect the expression of nemy isoforms. We show that the nemy (45) excision, which specifically reduces the expression of the longest splice form of nemy, leads to an increase in stimulus evoked transmitter release and altered synaptic plasticity at the NMJ. Conversely, the nemy (26.2) excision, which appears to reduce the expression of all splice forms except the longest splice isoform, shows a reduction in stimulus evoked transmitter release, and enhanced synaptic plasticity. We further show that nemy (45) mutants have reduced levels of amidated peptides similar to that observed in peptidyl-glycine hydryoxylating mono-oxygenase (PHM) mutants. In contrast, nemy (26.2) mutants show no defects in peptide amidation but rather display a decrease in Tyramine β hydroxylase activity (TβH). Taken together, these results show non-redundant roles for the different nemy isoforms and shed light on the complex regulation of neuromodulators. Public Library of Science 2015-08-03 /pmc/articles/PMC4523183/ /pubmed/26237434 http://dx.doi.org/10.1371/journal.pone.0132548 Text en © 2015 Knight et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Knight, David Iliadi, Konstantin G. Iliadi, Natalia Wilk, Ronit Hu, Jack Krause, Henry M. Taylor, Paul Moran, Michael F. Boulianne, Gabrielle L. Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy |
title | Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy
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title_full | Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy
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title_fullStr | Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy
|
title_full_unstemmed | Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy
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title_short | Distinct Regulation of Transmitter Release at the Drosophila NMJ by Different Isoforms of nemy
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title_sort | distinct regulation of transmitter release at the drosophila nmj by different isoforms of nemy |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4523183/ https://www.ncbi.nlm.nih.gov/pubmed/26237434 http://dx.doi.org/10.1371/journal.pone.0132548 |
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