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MBE Advance Access published online on November 6, 2009
Molecular Biology and Evolution, doi:10.1093/molbev/msp268
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© The Author 2009. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Research Article

Phylogenetic analysis of gene structure and alternative splicing in {alpha}-actinins

Monkol Lek1,2, Daniel G. MacArthur1,2,3, Nan Yang1,2 and Kathryn N. North1,2

1 Institute for Neuroscience and Muscle Research, The Children's Hospital at Westmead, Sydney 2145, NSW, Australia
2 Discipline of Paediatrics and Child Health, Faculty of Medicine, University of Sydney, Sydney 2006, NSW, Australia
3 Wellcome Trust Sanger Institute, Hinxton, CB10 1SA, UK

Corresponding Author Email: monkol.lek{at}gmail.com

Received for publication September 28, 2009. Revision received October 28, 2009. Accepted for publication October 29, 2009.

The {alpha}-actinins are an important family of actin-binding proteins with the ability to cross-link actin filaments when in dimer form. Members of the {alpha}-actinin family share a domain topology composed of highly conserved actin binding and EF-hand domains separated by a rod domain composed of spectrin-like repeats. Functional diversity within this family has arisen through exon duplication and the formation of alternate splice isoforms as well as gene duplications during the evolution of vertebrates. In addition to the known functional domains, {alpha}-actinins also contain a consensus PDZ binding site. The completed genome sequence of over 32 invertebrate species has allowed the analysis of gene structure and exon/gene duplication over a diverse range of phyla. Our analysis shows that relative to early branching metazoans, considerable intron loss especially in arthropods with few cases of intron gains. The C-terminal PDZ binding site is conserved in nearly all invertebrates but is missing in some nematodes and platyhelminths. Alternative splicing in the actin-binding domain is conserved in chordates, arthropods and some nematodes and platyhelminths. In contrast, alternative splicing of the EF-hand domain is only observed in chordates. Finally, given the prevalence of exon duplications seen in the actin-binding domain, this may act as a significant mechanism in the modification of actin binding properties.

Key Words: gene structure • gene/exon duplication • alternate splicing • {alpha}–actinins


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