ArticleThe EMBO journal1989
Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode.
Article in The EMBO journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 130 citations in OpenAlex.
- Nuclear roles for non-lamin intermediate filament proteins.Current opinion in cell biology · 2024Review
- Article
- A cytoplasmic escapee: desmin is going nuclear.Turkish journal of biology = Turk biyoloji dergisi · 2021Review
- Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity.Nature communications · 2019Article
- Evolutionary changes in lamin expression in the vertebrate lineage.Nucleus (Austin, Tex.) · 2017Article
- Ancient Eukaryotic Origin and Evolutionary Plasticity of Nuclear Lamina.Genome biology and evolution · 2016Article
- Nuclear membrane diversity: underlying tissue-specific pathologies in disease?Current opinion in cell biology · 2015Review
- Phosphorylation of lamins determine their structural properties and signaling functions.Nucleus (Austin, Tex.) · 2015Article
- The evolution of the cytoskeleton.The Journal of cell biology · 2011Review
- The lamin protein family.Genome biology · 2011Review
- Intermediate filaments: a historical perspective.Experimental cell research · 2007Review
- Biochemical and immunological characterization of pea nuclear intermediate filament proteins.Planta · 2004Article
- Essential roles for four cytoplasmic intermediate filament proteins in Caenorhabditis elegans development.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Conservation of matrix attachment region-binding filament-like protein 1 among higher plants.Plant physiology · 2000Article
- Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae.The Journal of cell biology · 1997Article
- Intermediate filaments as dynamic structures.Cancer metastasis reviews · 1996Review
- The gene structure of B-type nuclear lamins of Xenopus laevis: implications for the evolution of the vertebrate lamin family.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 1994Article
- Eight genes and alternative RNA processing pathways generate an unexpectedly large diversity of cytoplasmic intermediate filament proteins in the nematode Caenorhabditis elegans.The EMBO journal · 1994Article
- Onchocerca volvulus and Acanthocheilonema viteae: cloning of cDNAs for muscle-cell intermediate filaments.Parasitology research · 1994Article
- The roles of the rod end and the tail in vimentin IF assembly and IF network formation.The Journal of cell biology · 1993Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The giant body muscle cells of the nematode Ascaris lumbricoides show a complex three dimensional array of intermediate filaments (IFs). They contain two proteins, A (71 kd) and B (63 kd), which we now show are able to form homopolymeric filaments in vitro. The complete amino acid sequence of B and 80% of A have been determined. A and B are two homologous proteins with a 55% sequence identity over the rod and tail domains. Sequence comparisons with the only other invertebrate IF protein currently known (Helix pomatia) and with vertebrate IF proteins show that along the coiled-coil rod domain, sequence principles rather than actual sequences are conserved in evolution. Noticeable exceptions are the consensus sequences at the ends of the rod, which probably play a direct role in IF assembly. Like the Helix IF protein the nematode proteins have six extra heptads in the coil 1b segment. These are characteristic of nuclear lamins from vertebrates and invertebrates and are not found in vertebrate IF proteins. Unexpectedly the enhanced homology between lamins and invertebrate IF proteins continues in the tail domains, which in vertebrate IF proteins totally diverge. The sequence alignment necessitates the introduction of a 15 residue deletion in the tail domain of all three invertebrate IF proteins. Its location coincides with the position of the karyophilic signal sequence, which dictates nuclear entry of the lamins. The results provide the first molecular support for the speculation that nuclear lamins and cytoplasmic IF proteins arose in eukaryotic evolution from a common lamin-like predecessor.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.