English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/17782
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 44 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Título

Evolution of the insulin receptor family and receptor isoform expression in vertebrates

AutorHernández-Sánchez, Catalina ; Mansilla, Alicia ; Pablo, Flora de ; Zardoya, Rafael
Palabras claveInsulin receptor
Alternative splicing
Ancestral character states
Fecha de publicación29-feb-2008
EditorOxford University Press
CitaciónMolecular Biology and Evolution 25(6):1043-1053(2008)
ResumenThe molecular phylogeny of the vertebrate insulin receptor (IR) family was reconstructed under maximum likelihood (ML) to establish homologous relationships among its members. A sister group relationship between the orphan insulin–related receptor (IRR) and the insulin-like growth factor 1 receptor (IGF1R) to the exclusion of the IR obtained maximal bootstrap support. Although both IR and IGF1R were identified in all vertebrates, IRR could not be found in any teleost fish. The ancestral character states at each position of the receptor molecule were inferred for IR, IRR + IGF1R, and all 3 paralogous groups based on the recovered phylogeny using ML in order to determine those residues that could be important for the specific function of IR. For 18 residues, ancestral character state of IR was significantly distinct (probability >0.95) with respect to the corresponding inferred ancestral character states both of IRR + IGF1R and of all 3 vertebrate paralogs. Most of these IR distinct (shared derived) residues were located on the extracellular portion of the receptor (because this portion is larger and the rate of generation of IR shared derived sites is uniform along the receptor), suggesting that functional diversification during the evolutionary history of the family was largely generated modifying ligand affinity rather than signal transduction at the tyrosine kinase domain. In addition, 2 residues at positions 436 and 1095 of the human IR sequence were identified as radical cluster-specific sites in IRR + IGF1R. Both Ir and Irr have an extra exon (namely exon 11) with respect to Igf1r. We used the molecular phylogeny to infer the evolution of this additional exon. The Irr exon 11 can be traced back to amphibians, whereas we show that presence and alternative splicing of Ir exon 11 seems to be restricted exclusively to mammals. The highly divergent sequence of both exons and the reconstructed phylogeny of the vertebrate IR family strongly indicate that both exons were acquired independently by each paralog.
Descripción11 pages, 4 figures, 1 table.-- PMID: 18310661 [PubMed].-- Printed version published Jun 2008.
Full-text version available Open Access at the journal site.
Versión del editorhttp://dx.doi.org/10.1093/molbev/msn036
URIhttp://hdl.handle.net/10261/17782
DOI10.1093/molbev/msn036
ISSN0737-4038 (Print)
1537-1719 (Online)
Aparece en las colecciones: (CIB) Artículos
(MNCN) Artículos
Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.