ArticleBMC evolutionary biology2007
Molecular evolution of type VI intermediate filament proteins.
Article in BMC evolutionary biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.
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Who cites it
44 citing papers in PubMed, 1 synthesis or guideline pooled it, 95 citations in OpenAlex.
- Pooled it
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- Neuronal differentiation of human dental pulp stem cells induced by co-treatment of ergothioneine.PloS one · 2025Article
- Role of the cytoskeleton in cellular reprogramming: effects of biophysical and biochemical factors.Frontiers in molecular biosciences · 2025Review
- Non-contact confocal calcium imaging ofBiomedical optics express · 2025Article
- Bone marrow mesenchymal stem cells in treatment of peripheral nerve injury.World journal of stem cells · 2024Review
- The CRL3Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The intermediate filament protein nestin serves as a molecular hub for smooth muscle cytoskeletal signaling.Respiratory research · 2023Article
- Characterization of neural stem cells derived from human stem cells from the apical papilla undergoing three-dimensional neurosphere induction.Journal of applied oral science : revista FOB · 2023Article
- miR-204-5p inhibits cell proliferation and induces cell apoptosis in esophageal squamous cell carcinoma by regulating Nestin.International journal of medical sciences · 2022Article
- Article
- Stem-like cells drive NF1-associated MPNST functional heterogeneity and tumor progression.Cell stem cell · 2021Article
- The Impact of lncRNAs and miRNAs in Regulation of Function of Cancer Stem Cells and Progression of Cancer.Frontiers in cell and developmental biology · 2021Review
- Genetically Encoded Calcium Indicators for In Situ Functional Studies of Corneal Nerves.Investigative ophthalmology & visual science · 2020Article
- Review
- The Intermediate Filament Synemin Regulates Non-Homologous End Joining in an ATM-Dependent Manner.Cancers · 2020Article
- Synemin Redefined: Multiple Binding Partners Results in Multifunctionality.Frontiers in cell and developmental biology · 2020Review
- High NESTIN Expression Marks the Endosteal Capillary Network in Human Bone Marrow.Frontiers in cell and developmental biology · 2020Article
- Clinicopathological and prognostic significance of nestin expression in patients with breast cancer: a systematic review and meta-analysis.Cancer cell international · 2020Article
- Deer antler stem cells are a novel type of cells that sustain full regeneration of a mammalian organ-deer antler.Cell death & disease · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTanabin, transitin and nestin are type VI intermediate filament (IF) proteins that are developmentally regulated in frogs, birds and mammals, respectively. Tanabin is expressed in the growth cones of embryonic vertebrate neurons, whereas transitin and nestin are found in myogenic and neurogenic cells. Another type VI IF protein, synemin, is expressed in undifferentiated and mature muscle cells of birds and mammals. In addition to an IF-typical alpha-helical core domain, type VI IF proteins are characterized by a long C-terminal tail often containing distinct repeated motifs. The molecular evolution of type VI IF proteins remains poorly studied.
resultsTo examine the evolutionary history of type VI IF proteins, sequence comparisons, BLAST searches, synteny studies and phylogenic analyses were performed. This study provides new evidence that tanabin, transitin and nestin are indeed orthologous type VI IF proteins. It demonstrates that tanabin, transitin and nestin genes share intron positions and sequence identities, have a similar chromosomal context and display closely related positions in phylogenic analyses. Despite this homology, fast evolution rates of their C-terminal extremity have caused the appearance of repeated motifs with distinct biological activities. In particular, our in silico and in vitro analyses of their tail domain have shown that (avian) transitin, but not (mammalian) nestin, contains a repeat domain displaying nucleotide hydrolysis activity.
conclusionThese analyses of the evolutionary history of the IF proteins fit with a model in which type VI IFs form a branch distinct from NF proteins and are composed of two major proteins: synemin and nestin orthologs. Rapid evolution of the C-terminal extremity of nestin orthologs could be responsible for their divergent functions.
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