ArticleThe Journal of cell biology1997
Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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Who cites it
111 citing papers in PubMed, 281 citations in OpenAlex.
- Lamin-ating the genome: quantitative gatekeeping of replication initiation.Trends in cell biology · 2026Article
- Lamin A/C loss promotes R-loop-mediated genomic instability and poor survival in small-cell lung cancer.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Lamin A/C Deficiency Drives Genomic Instability and Poor Survival in Small-Cell Lung Cancer through Increased R-loop Accumulation.bioRxiv : the preprint server for biology · 2025Article
- RSK2 and its binding partners: an emerging signaling node in cancers.Archives of pharmacal research · 2025Review
- Role of Nuclear Lamins in the Regulation of the Genome: Focus on CardioLaminopathy.Sub-cellular biochemistry · 2025Review
- RSK2-mediated cGAS phosphorylation induces cGAS chromatin-incorporation-mediated cell transformation and cancer cell colony growth.Cell death discovery · 2024Article
- Lamin A/C facilitates DNA damage response by modulating ATM signaling and homologous recombination pathways.Animal cells and systems · 2024Article
- The Functions of Pt-DIC and Pt-Lamin B in Spermatogenesis ofInternational journal of molecular sciences · 2023Article
- Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023Review
- Loss of FAM111B protease mutated in hereditary fibrosing poikiloderma negatively regulates telomere length.Frontiers in cell and developmental biology · 2023Article
- The Nuclear Envelope as a Regulator of Immune Cell Function.Frontiers in immunology · 2022Review
- A nuclear enterprise: zooming in on nuclear organization and gene expression control in the African trypanosome.Parasitology · 2021Review
- Review
- Nuclear Envelope Integrity in Health and Disease: Consequences on Genome Instability and Inflammation.International journal of molecular sciences · 2021Review
- Progerin impairs 3D genome organization and induces fragile telomeres by limiting the dNTP pools.Scientific reports · 2021Article
- Review
- A Unified Linear Viscoelastic Model of the Cell Nucleus Defines the Mechanical Contributions of Lamins and Chromatin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Perinuclear Lamin A and Nucleoplasmic Lamin B2 Characterize Two Types of Hippocampal Neurons through Alzheimer's Disease Progression.International journal of molecular sciences · 2020Article
- Genomic instability and innate immune responses to self-DNA in progeria.GeroScience · 2019Review
- The Biology of the Nuclear Envelope and Its Implications in Cancer Biology.International journal of molecular sciences · 2019Review
51 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The nuclear lamina is a fibrous structure that lies at the interface between the nuclear envelope and the nucleoplasm. The major proteins comprising the lamina, the nuclear lamins, are also found in foci in the nucleoplasm, distinct from the peripheral lamina. The nuclear lamins have been associated with a number of processes in the nucleus, including DNA replication. To further characterize the specific role of lamins in DNA replication, we have used a truncated human lamin as a dominant negative mutant to perturb lamin organization. This protein disrupts the lamin organization of nuclei when microinjected into mammalian cells and also disrupts the lamin organization of in vitro assembled nuclei when added to Xenopus laevis interphase egg extracts. In both cases, the lamina appears to be completely absent, and instead the endogenous lamins and the mutant lamin protein are found in nucleoplasmic aggregates. Coincident with the disruption of lamin organization, there is a dramatic reduction in DNA replication. As a consequence of this disruption, the distributions of PCNA and the large subunit of the RFC complex, proteins required for the elongation phase of DNA replication, are altered such that they are found within the intranucleoplasmic lamin aggregates. In contrast, the distribution of XMCM3, XORC2, and DNA polymerase alpha, proteins required for the initiation stage of DNA replication, remains unaltered. The data presented demonstrate that the nuclear lamins may be required for the elongation phase of DNA replication.
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Registered trials
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.