ArticleThe EMBO journal1987
Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily.
Article in The EMBO journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 140 citations in OpenAlex.
- The Long Linker Region of Telomere-Binding Protein TRF2 Is Responsible for Interactions with Lamins.International journal of molecular sciences · 2021Article
- Mechanotransduction, nuclear architecture and epigenetics in Emery Dreifuss Muscular Dystrophy: tous pour un, un pour tous.Nucleus (Austin, Tex.) · 2018Review
- Generation and characterization of a conditional deletion allele for Lmna in mice.Biochemical and biophysical research communications · 2013Article
- Primary biliary cirrhosis: what do autoantibodies tell us?World journal of gastroenterology · 2010Review
- Molecular characterization of a novel, widespread nuclear protein that colocalizes with spliceosome components.Molecular biology of the cell · 1998Article
- Protein 4.1 is a component of the nuclear matrix of mammalian cells.The Biochemical journal · 1995Article
- Vimentin-associated mitotic vesicles interact with chromosomes in a lamin B- and phosphorylation-dependent manner.The EMBO journal · 1995Article
- 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
- Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: implications for nuclear reassembly.The EMBO journal · 1994Article
- Membrane-associated lamins in Xenopus egg extracts: identification of two vesicle populations.The Journal of cell biology · 1993Article
- The prosomal RNA-binding protein p27K is a member of the alpha-type human prosomal gene family.Molecular & general genetics : MGG · 1993Article
- The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins.The EMBO journal · 1992Article
- The gene structure of Xenopus nuclear lamin A: a model for the evolution of A-type from B-type lamins by exon shuffling.Chromosoma · 1992Article
- A normally masked nuclear matrix antigen that appears at mitosis on cytoskeleton filaments adjoining chromosomes, centrioles, and midbodies.The Journal of cell biology · 1992Article
- Molecular cloning of matrin F/G: A DNA binding protein of the nuclear matrix that contains putative zinc finger motifs.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase.The EMBO journal · 1991Article
- Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions.The Journal of cell biology · 1991Article
- The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2.The Journal of cell biology · 1991Article
- The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen.The EMBO journal · 1991Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lamins are karyoskeletal proteins associated with the nuclear envelope which can be divided into two groups, i.e. the type A lamins of near neutral pI and the more acidic lamins, including mammalian lamin B. We have isolated cDNA clones encoding a representative of the type B subfamily from Xenopus laevis, and have deduced its amino acid sequence from the coding portion of the approximately 2.9 kb mRNA. The polypeptide (mol. wt 66,433) is identified as a typical lamin by its homology to Xenopus human type A lamins, but detailed sequence comparison shows that LI is less related to Xenopus lamin A than the latter is to human lamin A. The conformation predicted for LI conforms to the general model of lamins and intermediate filament proteins and is characterized by an extended central alpha-helical coiled coil domain, flanked by non-alpha-helical domains, i.e. a relatively short N-terminal head and a long C-terminal tail. As in lamins A and C, the head of lamin LI is positively charged and the tail presents a similar C-terminal pentapeptide, a putative nuclear accumulation signal, a very negatively charged region and a number of short regions that are highly homologous in all lamins. However, LI differs from the type A lamins by the absence of the oligo-histidine stretch and a di-proline motif in the tail region and by a significantly lower number of identical amino acid positions.(ABSTRACT TRUNCATED AT 250 WORDS)
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