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dc.contributor.authorElphick, MR
dc.contributor.authorSemmens, DC
dc.contributor.authorBlowes, LM
dc.contributor.authorLevine, J
dc.contributor.authorLowe, CJ
dc.contributor.authorArnone, MI
dc.contributor.authorClark, MS
dc.description.abstractThe SALMFamides are a family of neuropeptides that act as muscle relaxants in echinoderms. Analysis of genome/transcriptome sequence data from the sea urchin Strongylocentrotus purpuratus (Echinoidea), the sea cucumber Apostichopus japonicus (Holothuroidea), and the starfish Patiria miniata (Asteroidea) reveals that in each species there are two types of SALMFamide precursor: an L-type precursor comprising peptides with a C-terminal LxFamide-type motif and an F-type precursor solely or largely comprising peptides with a C-terminal FxFamide-type motif. Here, we have identified transcripts encoding SALMFamide precursors in the brittle star Ophionotus victoriae (Ophiuroidea) and the feather star Antedon mediterranea (Crinoidea). We have also identified SALMFamide precursors in other species belonging to each of the five echinoderm classes. As in S. purpuratus, A. japonicus, and P. miniata, in O. victoriae there is one L-type precursor and one F-type precursor. However, in A. mediterranea only a single SALMFamide precursor was found, comprising two peptides with a LxFamide-type motif, one with a FxFamide-type motif, five with a FxLamide-type motif, and four with a LxLamide-type motif. As crinoids are basal to the Echinozoa (Holothuroidea + Echinoidea) and Asterozoa (Asteroidea + Ophiuroidea) in echinoderm phylogeny, one model of SALMFamide precursor evolution would be that ancestrally there was a single SALMFamide gene encoding a variety of SALMFamides (as in crinoids), which duplicated in a common ancestor of the Echinozoa and Asterozoa and then specialized to encode L-type SALMFamides or F-type SALMFamides. Alternatively, a second SALMFamide precursor may remain to be discovered or may have been lost in crinoids. Further insights will be obtained if SALMFamide receptors are identified, which would provide a molecular basis for experimental analysis of the functional significance of the "cocktails" of SALMFamides that exist in echinoderms.
dc.description.sponsorshipThis work was supported by a Ph.D. studentship awarded to Dean C. Semmens by Queen Mary University of London. Sequencing of the O. victoriae and A. mediterranea transcriptomes was funded by the Natural Environmental Research Council (NE-C300-62202-3215; British Antarctic Survey, Cambridge). This research was also supported by the National Institute for Health Research (NIHR) Biomedical Research Center based at Guy’s and St Thomas’ NHS Foundation Trust and King’s College London. The views expressed are those of the authors and not necessarily those of the NHS, the NIHR or the Department of Health. We are very grateful to Dr. Timothy O’Hara and Dr. Andrew Hugall (Museum Victoria, Melbourne, VIC, Australia) for providing access to their echinoderm transcriptome sequence data.en_US
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dc.relation.ispartofFront Endocrinol (Lausanne)
dc.rights© 2015 Elphick, Semmens, Blowes, Levine, Lowe, Arnone and Clark. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. This Document is protected by copyright and was first published by Frontiers. All rights reserved. It is reproduced with permission.
dc.titleReconstructing SALMFamide Neuropeptide Precursor Evolution in the Phylum Echinodermata: Ophiuroid and Crinoid Sequence Data Provide New Insights.
dc.typeJournal Article
dc.relation.isPartOfFrontiers in Endocrinology
dc.relation.isPartOfFront Endocrinol (Lausanne)
dc.relation.isPartOfFront Endocrinol (Lausanne)
pubs.organisational-group/Queen Mary University of London
pubs.organisational-group/Queen Mary University of London/Faculty of Science & Engineering
pubs.organisational-group/Queen Mary University of London/Faculty of Science & Engineering/Biological and Chemical Sciences - Biology - Research Students
pubs.organisational-group/Queen Mary University of London/Faculty of Science & Engineering/Biological and Chemical Sciences - Staff
pubs.organisational-group/Queen Mary University of London/Faculty Reporting - Research Students
pubs.organisational-group/Queen Mary University of London/Faculty Reporting - Research Students/Faculty of Science & Engineering PGRs
pubs.publication-statusPublished online

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