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Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex

BACKGROUND: The insulin signaling pathway (ISP) has a key role in major physiological events like carbohydrate metabolism and growth regulation. The ISP has been well described in vertebrates and in a few invertebrate model organisms but remains largely unexplored in non-model invertebrates. This st...

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Autores principales: Boucher, Philippe, Ditlecadet, Delphine, Dubé, Caroline, Dufresne, France
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2978223/
https://www.ncbi.nlm.nih.gov/pubmed/20939922
http://dx.doi.org/10.1186/1471-2148-10-305
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author Boucher, Philippe
Ditlecadet, Delphine
Dubé, Caroline
Dufresne, France
author_facet Boucher, Philippe
Ditlecadet, Delphine
Dubé, Caroline
Dufresne, France
author_sort Boucher, Philippe
collection PubMed
description BACKGROUND: The insulin signaling pathway (ISP) has a key role in major physiological events like carbohydrate metabolism and growth regulation. The ISP has been well described in vertebrates and in a few invertebrate model organisms but remains largely unexplored in non-model invertebrates. This study is the first detailed genomic study of this pathway in a crustacean species, Daphnia pulex. RESULTS: The Daphnia pulex draft genome sequence assembly was scanned for major components of the ISP with a special attention to the insulin-like receptor. Twenty three putative genes are reported. The pathway appears to be generally well conserved as genes found in other invertebrates are present. Major findings include a lower number of insulin-like peptides in Daphnia as compared to other invertebrates and the presence of multiple insulin-like receptors (InR), with four genes as opposed to a single one in other invertebrates. Genes encoding for the Dappu_InR are likely the result of three duplication events and bear some unusual features. Dappu_InR-4 has undergone extensive evolutionary divergence and lacks the conserved site of the catalytic domain of the receptor tyrosine kinase. Dappu_InR-1 has a large insert and lacks the transmembranal domain in the β-subunit. This domain is also absent in Dappu_InR-3. Dappu_InR-2 is characterized by the absence of the cystein-rich region. Real-time q-PCR confirmed the expression of all four receptors. EST analyses of cDNA libraries revealed that the four receptors were differently expressed under various conditions. CONCLUSIONS: Duplications of the insulin receptor genes might represent an important evolutionary innovation in Daphnia as they are known to exhibit extensive phenotypic plasticity in body size and in the size of defensive structures in response to predation.
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spelling pubmed-29782232010-11-11 Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex Boucher, Philippe Ditlecadet, Delphine Dubé, Caroline Dufresne, France BMC Evol Biol Research Article BACKGROUND: The insulin signaling pathway (ISP) has a key role in major physiological events like carbohydrate metabolism and growth regulation. The ISP has been well described in vertebrates and in a few invertebrate model organisms but remains largely unexplored in non-model invertebrates. This study is the first detailed genomic study of this pathway in a crustacean species, Daphnia pulex. RESULTS: The Daphnia pulex draft genome sequence assembly was scanned for major components of the ISP with a special attention to the insulin-like receptor. Twenty three putative genes are reported. The pathway appears to be generally well conserved as genes found in other invertebrates are present. Major findings include a lower number of insulin-like peptides in Daphnia as compared to other invertebrates and the presence of multiple insulin-like receptors (InR), with four genes as opposed to a single one in other invertebrates. Genes encoding for the Dappu_InR are likely the result of three duplication events and bear some unusual features. Dappu_InR-4 has undergone extensive evolutionary divergence and lacks the conserved site of the catalytic domain of the receptor tyrosine kinase. Dappu_InR-1 has a large insert and lacks the transmembranal domain in the β-subunit. This domain is also absent in Dappu_InR-3. Dappu_InR-2 is characterized by the absence of the cystein-rich region. Real-time q-PCR confirmed the expression of all four receptors. EST analyses of cDNA libraries revealed that the four receptors were differently expressed under various conditions. CONCLUSIONS: Duplications of the insulin receptor genes might represent an important evolutionary innovation in Daphnia as they are known to exhibit extensive phenotypic plasticity in body size and in the size of defensive structures in response to predation. BioMed Central 2010-10-12 /pmc/articles/PMC2978223/ /pubmed/20939922 http://dx.doi.org/10.1186/1471-2148-10-305 Text en Copyright ©2010 Boucher et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Boucher, Philippe
Ditlecadet, Delphine
Dubé, Caroline
Dufresne, France
Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex
title Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex
title_full Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex
title_fullStr Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex
title_full_unstemmed Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex
title_short Unusual duplication of the insulin-like receptor in the crustacean Daphnia pulex
title_sort unusual duplication of the insulin-like receptor in the crustacean daphnia pulex
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2978223/
https://www.ncbi.nlm.nih.gov/pubmed/20939922
http://dx.doi.org/10.1186/1471-2148-10-305
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