ArticleChromosoma1992
The gene structure of Xenopus nuclear lamin A: a model for the evolution of A-type from B-type lamins by exon shuffling.
Article in Chromosoma, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- Advances in research on the relationship between the LMNA gene and human diseases (Review).Molecular medicine reports · 2024Review
- Nuclear Lamins: Key Proteins for Embryonic Development.Biology · 2022Review
- Cell cycle-dependent dynamics of a plant intermediate filament motif protein with intracellular localization related to microtubules.Protoplasma · 2020Article
- Do lamin A and lamin C have unique roles?Chromosoma · 2015Review
- The tail domain of lamin B1 is more strongly modulated by divalent cations than lamin A.Nucleus (Austin, Tex.) · 2015Article
- The lamin protein family.Genome biology · 2011Review
- Biochemical and immunological characterization of pea nuclear intermediate filament proteins.Planta · 2004Article
- The tail domain of lamin Dm0 binds histones H2A and H2B.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- 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
- The role of CaaX-dependent modifications in membrane association of Xenopus nuclear lamin B3 during meiosis and the fate of B3 in transfected mitotic cells.The Journal of cell biology · 1993Article
- Membrane-associated lamins in Xenopus egg extracts: identification of two vesicle populations.The Journal of cell biology · 1993Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear lamins are intermediate filament (IF) type proteins that form a fibrillar network underlying the inner nuclear membrane. The existence of multiple subtypes of lamins in vertebrates has been interpreted in terms of functional specialization during cell division and differentiation. The structure of a gene encoding an A-type lamin of Xenopus laevis was analysed. Comparison with that of a B-type lamin of the same species shows remarkable conservation of the exon/intron pattern. In both genes the last exon, only 9-12 amino acids in length, encodes the complete information necessary for membrane targeting of lamins, i.e. a ras-related CaaX motif. The lamin A specific extension of the tail domain is encoded by a single additional exon. The 5' boundary of this exon coincides with the sequence divergence between human lamins A and C, for which an alternative splice mechanism had previously been suggested. Arguments are presented suggesting that B-type lamins represent the ancestral type of lamins and that A-type lamins derived there from by exon shuffling. The acquisition of the new exon might explain the different fates of A- and B-types lamins during cell division.
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