ArticleThe Journal of cell biology2001
Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization.
Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 132 citations in OpenAlex.
- Review
- Nuclear Envelope Dynamics inCells · 2025Review
- Advances in research on the relationship between the LMNA gene and human diseases (Review).Molecular medicine reports · 2024Review
- Article
- Comparative membrane proteomics reveals diverse cell regulators concentrated at the nuclear envelope.Life science alliance · 2023Article
- Review
- Genomic analysis of an ultrasmall freshwater green alga, Medakamo hakoo.Communications biology · 2023Article
- Slower diffusion and anomalous association of R453W lamin A protein alter nuclear architecture in AD-EDMD.RSC advances · 2022Article
- Nuclear peripheral chromatin-lamin B1 interaction is required for global integrity of chromatin architecture and dynamics in human cells.Protein & cell · 2022Article
- Genomic loci mispositioning in Tmem120a knockout mice yields latent lipodystrophy.Nature communications · 2022Article
- Subnuclear gene positioning through lamina association affects copper tolerance.Nature communications · 2020Article
- Lamin A/C Mechanotransduction in Laminopathies.Cells · 2020Review
- Article
- The cell-wide web coordinates cellular processes by directing site-specific CaNature communications · 2019Article
- Disrupting the LINC complex in smooth muscle cells reduces aortic disease in a mouse model of Hutchinson-Gilford progeria syndrome.Science translational medicine · 2018Article
- Extreme nuclear branching in healthy epidermal cells of theJournal of cell science · 2018Article
- Article
- Article
- Diseases of the Nucleoskeleton.Comprehensive Physiology · 2016Review
- B-type nuclear lamin and the nuclear pore complex Nup107-160 influences maintenance of the spindle envelope required for cytokinesis in Drosophila male meiosis.Biology open · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nuclear lamina is a meshwork of intermediate-type filament proteins (lamins) that lines the inner nuclear membrane. The lamina is proposed to be an important determinant of nuclear structure, but there has been little direct testing of this idea. To investigate lamina functions, we have characterized a novel lamin B1 mutant lacking the middle approximately 4/5 of its alpha-helical rod domain. Though retaining only 10 heptads of the rod, this mutant assembles into intermediate filament-like structures in vitro. When expressed in cultured cells, it concentrates in patches at the nuclear envelope. Concurrently, endogenous lamins shift from a uniform to a patchy distribution and lose their complete colocalization, and nuclei become highly lobulated. In vitro binding studies suggest that the internal rod region is important for heterotypic associations of lamin B1, which in turn are required for proper organization of the lamina. Accompanying the changes in lamina structure induced by expression of the mutant, nuclear pore complexes and integral membrane proteins of the inner membrane cluster, principally at the patches of endogenous lamins. Considered together, these data indicate that lamins play a major role in organizing other proteins in the nuclear envelope and in determining nuclear shape.
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Registered trials
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