ArticleNucleus (Austin, Tex.)
Disruption of lamin B1 and lamin B2 processing and localization by farnesyltransferase inhibitors.
Article in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 55 citations in OpenAlex.
- Lamin B1 safeguards the B cell genome and shapes lymphoma outcome.HemaSphere · 2026Article
- Increased Telomere Mobility in Progeria is Restored by Isoprenylcysteine Carboxyl Methyltransferase Inhibition.bioRxiv : the preprint server for biology · 2026Article
- Cancer-associated SPOP mutations enlarge nuclear size and facilitate nuclear envelope rupture upon farnesyltransferase inhibitor treatment.The Journal of clinical investigation · 2025Article
- Protein Prenylation in Plants: Mechanisms and Functional Implications.Plants (Basel, Switzerland) · 2025Review
- Baricitinib and Lonafarnib Synergistically Target Progerin and Inflammation, Improving Lifespan and Health in Progeria Mice.International journal of molecular sciences · 2025Article
- The Strange Case of the Noncanonical Lamina: Deep Divisions in Nuclear Organisation?Sub-cellular biochemistry · 2025Review
- Roles of the lamin A-specific tail region in the localization to sites of nuclear envelope rupture.PNAS nexus · 2024Article
- Non-random spatial organization of telomeres varies during the cell cycle and requires LAP2 and BAF.iScience · 2024Article
- Farnesyl-transferase inhibitors show synergistic anticancer effects in combination with novel KRAS-G12C inhibitors.British journal of cancer · 2024Article
- DNA damage induces nuclear envelope rupture through ATR-mediated phosphorylation of lamin A/C.Molecular cell · 2023Article
- Article
- Regulation of Lipid Metabolism by Lamin in Mutation-Related Diseases.Frontiers in pharmacology · 2022Review
- Lamin post-translational modifications: emerging toggles of nuclear organization and function.Trends in biochemical sciences · 2021Review
- Article
- Baricitinib, a JAK-STAT Inhibitor, Reduces the Cellular Toxicity of the Farnesyltransferase Inhibitor Lonafarnib in Progeria Cells.International journal of molecular sciences · 2021Article
- Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Regulation of Nuclear Mechanics and the Impact on DNA Damage.International journal of molecular sciences · 2021Review
- Diversity of Nuclear Lamin A/C Action as a Key to Tissue-Specific Regulation of Cellular Identity in Health and Disease.Frontiers in cell and developmental biology · 2021Review
- EZH2 reduction is an essential mechanoresponse for the maintenance of super-enhancer polarization against compressive stress in human periodontal ligament stem cells.Cell death & disease · 2020Article
- Nuclear envelope rupture and NET formation is driven by PKCα-mediated lamin B disassembly.EMBO reports · 2020Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Lamin A and the B-type lamins, lamin B1 and lamin B2, are translated as pre-proteins that are modified at a carboxyl terminal CAAX motif by farnesylation, proteolysis and carboxymethylation. Lamin A is further processed by proteolysis to remove the farnesyl, but B-type lamins remain permanently farnesylated. Two childhood diseases, Hutchinson Gilford Progeria Syndrome and restrictive dermopathy are caused by defects in the processing of lamin A, resulting in permanent farnesylation of the protein. Farnesyltransferase inhibitors, originally developed to target oncogenic Ras, have recently been used in clinical trials to treat children with Hutchinson Gilford Progeria Syndrome. Lamin B1 and lamin B2 play important roles in cell proliferation and organ development, but little is known about the role of farnesylation in their functions. Treating normal human fibroblasts with farnesyltransferase inhibitors causes the accumulation of unprocessed lamin B2 and lamin A and a decrease in mature lamin B1. Normally, lamins are concentrated at the nuclear envelope/lamina, but when farnesylation is inhibited, the peripheral localization of lamin B2 decreases as its nucleoplasmic levels increase. Unprocessed prelamin A distributes into both the nuclear envelope/lamina and nucleoplasm. Farnesyltransferase inhibitors also cause a rapid cell cycle arrest leading to cellular senescence. This study suggests that the long-term inhibition of protein farnesylation could have unforeseen consequences on nuclear functions.
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