Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes

BMC Evolutionary Biology

Research Article

Peter F. Stadler¹  Henrike Indrischek²  Sonja J. Prohaska³  Eugenia V. Gurevich⁴  Vsevolod V. Gurevich⁴ 

[1] Bioinformatics Group, Department of Computer Science, Universität Leipzig, Härtelstraße 16–18, D-04107, Leipzig, Germany;Interdisciplinary Center for Bioinformatics, Universität Leipzig, Härtelstraße 16–18, D-04107, Leipzig, Germany;Max Planck Institute for Mathematics in the Sciences, Inselstraße 22, D-04103, Leipzig, Germany;Fraunhofer Institute for Cell Therapy and Immunology, Perlickstraße 1, D-04103, Leipzig, Germany;Department of Theoretical Chemistry, University of Vienna, Währinger Straße 17, A-1090, Vienna, Austria;Center for non-coding RNA in Technology and Health, Grønegårdsvej 3, DK-1870, Frederiksberg C, Denmark;Santa Fe Institute, 1399 Hyde Park Rd., NM 87501, Santa Fe, USA;Computational EvoDevo Group, Department of Computer Science, Universität Leipzig, Härtelstraße 16–18, D-04107, Leipzig, Germany;Bioinformatics Group, Department of Computer Science, Universität Leipzig, Härtelstraße 16–18, D-04107, Leipzig, Germany;Interdisciplinary Center for Bioinformatics, Universität Leipzig, Härtelstraße 16–18, D-04107, Leipzig, Germany;Computational EvoDevo Group, Department of Computer Science, Universität Leipzig, Härtelstraße 16–18, D-04107, Leipzig, Germany;Interdisciplinary Center for Bioinformatics, Universität Leipzig, Härtelstraße 16–18, D-04107, Leipzig, Germany;Department of Pharmacology, Vanderbilt University, 2200 Pierce Ave, TN 37232, Nashville, USA;

关键词: Arrestin;    Signaling;    Gene duplication;    Evolution;    Receptor specificity;    Retrogene;   

DOI  :  10.1186/s12862-017-1001-4

 received in 2016-11-14, accepted in 2017-06-19,  发布年份 2017

来源: Springer

【 摘 要 】

BackgroundThe cytosolic arrestin proteins mediate desensitization of activated G protein-coupled receptors (GPCRs) via competition with G proteins for the active phosphorylated receptors. Arrestins in active, including receptor-bound, conformation are also transducers of signaling. Therefore, this protein family is an attractive therapeutic target. The signaling outcome is believed to be a result of structural and sequence-dependent interactions of arrestins with GPCRs and other protein partners. Here we elucidated the detailed evolution of arrestins in deuterostomes.ResultsIdentity and number of arrestin paralogs were determined searching deuterostome genomes and gene expression data. In contrast to standard gene prediction methods, our strategy first detects exons situated on different scaffolds and then solves the problem of assigning them to the correct gene. This increases both the completeness and the accuracy of the annotation in comparison to conventional database search strategies applied by the community. The employed strategy enabled us to map in detail the duplication- and deletion history of arrestin paralogs including tandem duplications, pseudogenizations and the formation of retrogenes. The two rounds of whole genome duplications in the vertebrate stem lineage gave rise to four arrestin paralogs. Surprisingly, visual arrestin ARR3 was lost in the mammalian clades Afrotheria and Xenarthra. Duplications in specific clades, on the other hand, must have given rise to new paralogs that show signatures of diversification in functional elements important for receptor binding and phosphate sensing.ConclusionThe current study traces the functional evolution of deuterostome arrestins in unprecedented detail. Based on a precise re-annotation of the exon-intron structure at nucleotide resolution, we infer the gain and loss of paralogs and patterns of conservation, co-variation and selection.

【 授权许可】

CC BY   
© The Author(s) 2017

【 图 表 】

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