ArticleMolecular biology and evolution2010
Phylogenetic analysis of gene structure and alternative splicing in alpha-actinins.
Article in Molecular biology and evolution, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Exonic splicing code and protein binding sites for calcium.Nucleic acids research · 2022Article
- Evolutionarily diverse LIM domain-containing proteins bind stressed actin filaments through a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The protein subunit of telomerase displays patterns of dynamic evolution and conservation across different metazoan taxa.BMC evolutionary biology · 2017Article
- Structure and calcium-binding studies of calmodulin-like domain of human non-muscle α-actinin-1.Scientific reports · 2016Article
- The actinin family of actin cross-linking proteins - a genetic perspective.Cell & bioscience · 2015Article
- Phyletic distribution of fatty acid-binding protein genes.PloS one · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
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, there has been 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.
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